The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
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We are interested in where in or outside the cell the gene product carries out its function.
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Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
KCR1 (gene locus At1g67730, UniProt accession Q8L9C4) encodes very-long-chain 3-oxoacyl-CoA reductase 1 (β-ketoacyl-CoA reductase 1) in Arabidopsis thaliana (beaudoin2009functionalcharacterizationof pages 2-4, beaudoin2009functionalcharacterizationof pages 11-13). This 318-amino-acid, 35.7-kDa protein is the functional ketoacyl-CoA reductase component of the endoplasmic reticulum (ER)-localized fatty acid elongase (FAE) complex that produces very-long-chain fatty acids (VLCFAs, >18 carbons) (beaudoin2009functionalcharacterizationof pages 1-2, beaudoin2009functionalcharacterizationof pages 2-4). While UniProt lists "GLOSSY 8" (GL8) as an alternative name, the primary scientific literature uses GL8/GLOSSY8 predominantly to designate the maize orthologs GL8A and GL8B, which share approximately 55-56% amino-acid identity with Arabidopsis KCR1 (beaudoin2009functionalcharacterizationof pages 2-4, zheng2019co‐expressionanalysisaids pages 1-4). Therefore, cross-species nomenclature should be interpreted with care.
| Property | Evidence-based annotation |
|---|---|
| Target identity | Arabidopsis thaliana KCR1, locus At1g67730; UniProt Q8L9C4; encodes very-long-chain 3-oxoacyl-CoA reductase 1 (β-ketoacyl-CoA reductase 1), the functional KCR of the microsomal fatty-acid elongase (FAE) system (beaudoin2009functionalcharacterizationof pages 2-4, beaudoin2009functionalcharacterizationof pages 11-13) |
| Nomenclature caveat | UniProt lists GL8/GLOSSY8 as an alternative name, but primary literature generally uses GL8A/GL8B for maize homologs, not as the principal Arabidopsis locus name. AtKCR1 shares approximately 55–56% amino-acid identity with maize GL8A/GL8B; therefore, cross-species “GL8” literature should not be treated as direct evidence for AtKCR1 without verification (beaudoin2009functionalcharacterizationof pages 2-4, zheng2019co‐expressionanalysisaids pages 1-4) |
| Protein size and family features | Predicted 318-amino-acid, 35.7-kDa oxidoreductase. Sequence features include a putative dinucleotide-binding site and the conserved Ser–Tyr–Lys catalytic residues characteristic of short-chain dehydrogenase/reductase chemistry (beaudoin2009functionalcharacterizationof pages 2-4) |
| Primary enzymatic function | Catalyzes the first reductive step of each VLCFA-elongation cycle: 3-oxoacyl-CoA + NAD(P)H + H⁺ → 3-hydroxyacyl-CoA + NAD(P)⁺. This follows KCS-catalyzed condensation and precedes PAS2/HCD-catalyzed dehydration and CER10/ECR-catalyzed reduction (beaudoin2009functionalcharacterizationof pages 1-2, batsale2021biosynthesisandfunctions pages 3-5) |
| Substrate specificity | Acts on 3-oxoacyl-CoA intermediates generated during elongation of long-chain acyl-CoAs into VLCFAs. Available evidence supports broad chain-length acceptance; the associated KCS isoenzyme—not KCR1—principally determines acyl-chain-length specificity. No rigorous KCR1-specific kinetic preference series has been reported (batsale2021biosynthesisandfunctions pages 3-5, batsale2023tacklingfunctionalredundancy pages 1-2, lee2013recentadvancesin pages 1-2) |
| Cofactor requirement | Reduction requires a nicotinamide cofactor. Reviews commonly describe plant KCR activity as NAD(P)H-dependent or NADPH-dependent, whereas KCR1 sequence analysis identified a putative NADH-binding site. Direct comparative kinetics establishing strict NADH versus NADPH preference remain unavailable, so NAD(P)H is the most defensible designation (batsale2021biosynthesisandfunctions pages 3-5, beaudoin2009functionalcharacterizationof pages 11-13, beaudoin2009functionalcharacterizationof pages 2-4) |
| Subcellular localization | Endoplasmic reticulum/microsomal membrane system, where plant VLCFA elongation occurs. YFP–AtKCR1 fluorescence colocalized with ER markers in Arabidopsis and transiently transformed tobacco leaves (beaudoin2009functionalcharacterizationof pages 4-6, beaudoin2009functionalcharacterizationof pages 1-2) |
| ER-retention feature | AtKCR1 contains an apparent dilysine ER-retention motif, consistent with its experimentally observed ER localization; no evidence supports mitochondrial localization (beaudoin2009functionalcharacterizationof pages 2-4) |
| FAE-complex organization | Functions with a chain-length-selective KCS, PAS2/HCD, and CER10/ECR in a four-enzyme ER FAE system. Different KCS isoenzymes are thought to recruit or share the broadly acting KCR1–HCD–ECR core (batsale2023tacklingfunctionalredundancy pages 3-4, beaudoin2009functionalcharacterizationof pages 1-2, batsale2023tacklingfunctionalredundancy pages 1-2) |
| Protein interactions | Interaction studies summarized for Arabidopsis support a KCR-containing core with HCD and ECR and associations with the scaffold/chaperone PAS1 and accessory CER2. Because some assays label the protein generically as “KCR,” these interactions should be regarded as supportive of KCR1-complex organization rather than uniformly proven as KCR1-specific direct binding (xu2023proteininteractomesfor pages 3-4, batsale2021biosynthesisandfunctions pages 5-6) |
| Functional validation | AtKCR1, but not AtKCR2, restores elongase activity in the yeast ybr159Δ KCR mutant. AtKCR2 also fails to rescue Arabidopsis kcr1 embryo lethality, supporting KCR1 as the essential functional microsomal isoform (beaudoin2009functionalcharacterizationof pages 11-13, beaudoin2009functionalcharacterizationof pages 6-8) |
| Expression pattern | Broadly expressed in roots, leaves, inflorescence stems, flowers, siliques, seedlings, and developing embryos, with particularly strong expression in flowers and siliques. Unlike KCR2, KCR1 transcript is readily detected in roots and predominates during embryogenesis (beaudoin2009functionalcharacterizationof pages 6-8, beaudoin2009functionalcharacterizationof pages 4-6, beaudoin2009functionalcharacterizationof pages 1-2) |
| Metabolic outputs | Supplies VLCFAs for cuticular waxes, sphingolipids, suberin-associated lipids, seed triacylglycerols, and root glycerolipids. It is therefore a shared upstream VLCFA-supply enzyme rather than a wax-specific catalyst (beaudoin2009functionalcharacterizationof pages 1-2, batsale2021biosynthesisandfunctions pages 3-5) |
| Complete loss-of-function phenotype | Homozygous insertional loss of KCR1 is embryo lethal, demonstrating an essential requirement for KCR1-dependent VLCFA synthesis during embryogenesis (beaudoin2009functionalcharacterizationof pages 6-8, beaudoin2009functionalcharacterizationof pages 13-15) |
| Partial-loss phenotypes | RNAi suppression produces severity-dependent dwarfism, twisted or fused organs, abnormal flowers and siliques, reduced fertility, seed abortion, abnormal roots and root hairs, defective trichomes, swollen epidermal cells, and dehydration sensitivity (beaudoin2009functionalcharacterizationof pages 8-10, beaudoin2009functionalcharacterizationof pages 6-8) |
| Glossy/cuticle phenotype | Strongly suppressed plants develop glossy inflorescence stems lacking normal epicuticular wax crystals and show increased cuticle permeability. In severe RNAi lines, total stem wax was only 11.4% or 3.9% of wild type; weaker nonglossy lines retained approximately 75–80% (beaudoin2009functionalcharacterizationof pages 10-11) |
| Lipid-composition phenotype | KCR1 suppression reduces root C20, C22, and C24 fatty acids, lowers seed-oil VLCFAs by approximately 30% in severe lines, and decreases many sphingolipid species, linking the developmental phenotype to disruption of several VLCFA-dependent lipid pools (beaudoin2009functionalcharacterizationof pages 11-13, beaudoin2009functionalcharacterizationof pages 10-11) |
Table: Evidence-based summary of the identity, catalytic role, localization, complex membership, expression, and loss-of-function consequences of Arabidopsis KCR1. It also flags unresolved cofactor specificity and the potentially misleading cross-species GL8 nomenclature.
KCR1 catalyzes the first reduction step in each iterative cycle of very-long-chain fatty acid elongation (beaudoin2009functionalcharacterizationof pages 1-2, batsale2021biosynthesisandfunctions pages 3-5). The reaction converts β-ketoacyl-CoA (3-oxoacyl-CoA) intermediates to β-hydroxyacyl-CoA (3-hydroxyacyl-CoA) using NAD(P)H as a reducing cofactor:
3-oxoacyl-CoA + NAD(P)H + H⁺ → 3-hydroxyacyl-CoA + NAD(P)⁺
This reduction occurs immediately after the condensation reaction catalyzed by 3-ketoacyl-CoA synthase (KCS), which adds a two-carbon unit from malonyl-CoA to a long-chain acyl-CoA substrate (batsale2021biosynthesisandfunctions pages 3-5). Following KCR1-mediated reduction, the hydroxyacyl-CoA is dehydrated by 3-hydroxyacyl-CoA dehydratase (HCD/PAS2) to form an enoyl-CoA, which is then reduced by enoyl-CoA reductase (ECR/CER10) to complete the elongation cycle (batsale2021biosynthesisandfunctions pages 3-5).
KCR1 contains conserved Ser-Tyr-Lys catalytic residues characteristic of the short-chain dehydrogenase/reductase (SDR) family and possesses a putative dinucleotide-binding site (beaudoin2009functionalcharacterizationof pages 2-4). Although sequence analysis identified a putative NADH-binding site, the literature commonly describes plant KCR activity as NAD(P)H-dependent, and direct comparative kinetic measurements establishing strict NADH versus NADPH preference are not available (batsale2021biosynthesisandfunctions pages 3-5, beaudoin2009functionalcharacterizationof pages 11-13, beaudoin2009functionalcharacterizationof pages 2-4). The protein also contains a dilysine ER-retention motif consistent with its membrane localization (beaudoin2009functionalcharacterizationof pages 2-4).
KCR1 exhibits broad substrate specificity with respect to acyl-chain length, acting on β-ketoacyl-CoA intermediates generated during elongation of C16 and C18 fatty acids into VLCFAs ranging from C20 to C34 (batsale2021biosynthesisandfunctions pages 3-5, batsale2023tacklingfunctionalredundancy pages 1-2, lee2013recentadvancesin pages 1-2). Unlike the KCS condensing enzymes, which determine the chain-length substrate specificity of individual FAE complexes, KCR1 functions as a broadly acting, shared component with low genetic diversity (batsale2021biosynthesisandfunctions pages 3-5, batsale2023tacklingfunctionalredundancy pages 1-2). This broad specificity allows KCR1 to participate in multiple FAE complexes that differ primarily in their associated KCS isoform, thereby enabling production of the diverse VLCFA chain lengths required throughout the plant (batsale2023tacklingfunctionalredundancy pages 1-2).
Complementation experiments in yeast definitively established KCR1 as the functional microsomal KCR in Arabidopsis. AtKCR1, but not the related AtKCR2 protein, restores fatty acid elongation activity in the yeast ybr159Δ KCR mutant (beaudoin2009functionalcharacterizationof pages 11-13, beaudoin2009functionalcharacterizationof pages 6-8). Furthermore, AtKCR2 cannot rescue the embryo-lethal phenotype of Arabidopsis kcr1 null mutants, confirming that KCR1 is the essential KCR isoform for microsomal VLCFA biosynthesis (beaudoin2009functionalcharacterizationof pages 11-13).
KCR1 is localized to the endoplasmic reticulum (ER) membrane, where it functions as part of the ER-associated microsomal fatty acid elongase complex (beaudoin2009functionalcharacterizationof pages 4-6, beaudoin2009functionalcharacterizationof pages 1-2, beaudoin2009functionalcharacterizationof pages 11-13). Experimental evidence from fluorescent protein localization studies demonstrated that YFP-AtKCR1 fusion proteins colocalize with ER markers in both Arabidopsis leaves and transiently transformed tobacco leaves (beaudoin2009functionalcharacterizationof pages 4-6, beaudoin2009functionalcharacterizationof pages 1-2). The presence of a dilysine ER-retention motif in the KCR1 sequence provides additional sequence-based support for ER localization (beaudoin2009functionalcharacterizationof pages 2-4). The ER represents the exclusive site of VLCFA elongation in plants, and no evidence supports mitochondrial or other organellar localization of KCR1 (beaudoin2009functionalcharacterizationof pages 11-13, batsale2023tacklingfunctionalredundancy pages 2-3).
KCR1 functions within a multi-enzyme ER membrane complex comprising four core catalytic components: a chain-length-selective KCS enzyme, KCR1, PAS2 (HCD), and CER10 (ECR) (batsale2023tacklingfunctionalredundancy pages 3-4, beaudoin2009functionalcharacterizationof pages 1-2, batsale2023tacklingfunctionalredundancy pages 1-2). These enzymes catalyze four successive reactions in each two-carbon elongation cycle. The Arabidopsis genome encodes 21 KCS genes but only one or two genes for each of the other core enzymes, consistent with a model in which different KCS proteins define distinct FAE complexes that share the broadly acting KCR1, HCD, and ECR machinery (batsale2023tacklingfunctionalredundancy pages 1-2, batsale2021biosynthesisandfunctions pages 5-6).
Recent protein interaction studies support the organization of KCR within a core complex. Bimolecular fluorescence complementation (BiFC) and affinity-purification experiments detected interactions between KCR, ECR, and HCD, as well as associations with the scaffold/chaperone protein PAS1 (xu2023proteininteractomesfor pages 3-4). Split-luciferase complementation assays also identified interactions between CER2 (a BAHD-family accessory protein) and KCR, suggesting that CER2 may help organize or regulate elongase complexes (xu2023proteininteractomesfor pages 3-4). However, many of these interaction studies label the protein generically as "KCR" without distinguishing KCR1 from KCR2, so these should be regarded as supportive evidence for KCR1-complex organization rather than uniformly proven KCR1-specific direct binding interactions (xu2023proteininteractomesfor pages 3-4, batsale2021biosynthesisandfunctions pages 5-6).
KCR1 is broadly and constitutively expressed throughout Arabidopsis development (beaudoin2009functionalcharacterizationof pages 6-8, beaudoin2009functionalcharacterizationof pages 4-6, beaudoin2009functionalcharacterizationof pages 1-2). Transcript analysis by RT-PCR and promoter-GUS reporter assays detected KCR1 expression in roots, leaves, inflorescence stems, flowers, siliques, seedlings, and developing embryos, with particularly strong expression in flowers and siliques (beaudoin2009functionalcharacterizationof pages 6-8, beaudoin2009functionalcharacterizationof pages 4-6). Unlike AtKCR2, whose transcript is nearly undetectable in roots, AtKCR1 shows high transcript levels in root tissues (beaudoin2009functionalcharacterizationof pages 6-8, beaudoin2009functionalcharacterizationof pages 1-2). During embryogenesis, AtKCR1 expression is higher than AtKCR2 throughout development, consistent with KCR1 being the predominant and essential KCR isoform during this critical developmental stage (beaudoin2009functionalcharacterizationof pages 6-8).
KCR1 occupies a central position in plant lipid metabolism by supplying VLCFAs for multiple downstream pathways rather than serving a single specialized function (beaudoin2009functionalcharacterizationof pages 1-2, batsale2021biosynthesisandfunctions pages 3-5, batsale2021biosynthesisandfunctions pages 5-6). The VLCFAs produced through KCR1-dependent elongation are incorporated into several major lipid classes:
KCR1 supplies C20-C34 VLCFA precursors that are converted through wax biosynthetic pathways into aldehydes, alkanes, primary and secondary alcohols, ketones, and wax esters that form the epicuticular wax layer (beaudoin2009functionalcharacterizationof pages 1-2, lee2013recentadvancesin pages 1-2). In the FAE pathway for wax biosynthesis, KCR1 catalyzes the β-ketoacyl-CoA reduction step in each elongation cycle that generates the requisite VLCFA substrates (lee2013recentadvancesin pages 1-2). These waxes form the hydrophobic aerial barrier that limits non-stomatal water loss, provides protection against UV radiation and pathogens, and mediates plant-environment interactions (beaudoin2009functionalcharacterizationof pages 1-2).
VLCFAs constitute nearly 80% of sphingolipid fatty-acid chains in Arabidopsis, with C22-C26 chains being particularly prevalent (beaudoin2009functionalcharacterizationof pages 11-13, batsale2021biosynthesisandfunctions pages 13-14). KCR1-dependent elongation supplies these VLCFA precursors for ceramide synthesis by ceramide synthases such as LOH1 and LOH3, which preferentially use VLCFAs (batsale2021biosynthesisandfunctions pages 13-14). Sphingolipids are essential components of the plasma membrane outer leaflet and play crucial roles in membrane organization, membrane domain structure, intercellular communication, and signaling (batsale2021biosynthesisandfunctions pages 3-5). Reduced KCR1 activity causes a moderate but statistically significant decrease in nearly all measured sphingolipid species, linking normal sphingolipid homeostasis to KCR1 function (beaudoin2009functionalcharacterizationof pages 11-13).
KCR1 supplies VLCFA precursors for suberin-associated lipids, including ω-hydroxy fatty acids, dicarboxylic acids, fatty alcohols, and related compounds that form the hydrophobic root and periderm barriers (beaudoin2009functionalcharacterizationof pages 11-13, batsale2021biosynthesisandfunctions pages 3-5). These barriers govern water loss, solute movement, nutrient homeostasis, and environmental protection. Reduced KCR1 activity lowers C20, C22, and C24 fatty acids in roots and produces atypical oxygenated and dicarboxylic fatty acid products, consistent with impaired elongation and altered root lipid metabolism (beaudoin2009functionalcharacterizationof pages 11-13). Suberin biosynthesis is induced by drought, waterlogging, and nematode infection, suggesting roles in stress adaptation and defense (batsale2021biosynthesisandfunctions pages 13-14).
KCR1 supplies elongated acyl chains that are incorporated into seed triacylglycerols and root glycerolipids (beaudoin2009functionalcharacterizationof pages 1-2, batsale2021biosynthesisandfunctions pages 3-5). Strong KCR1 knockdown reduces seed oil VLCFA content by approximately 30% and alters the fatty acid composition of root glycerolipids (beaudoin2009functionalcharacterizationof pages 1-2, beaudoin2009functionalcharacterizationof pages 10-11). These contributions support storage lipid composition, germination-related reserves, and root membrane lipid homeostasis (beaudoin2009functionalcharacterizationof pages 1-2, batsale2021biosynthesisandfunctions pages 5-6).
VLCFAs are found in specific membrane phospholipids, particularly phosphatidylserine and phosphatidylethanolamine, where they may play roles in membrane domain organization and interleaflet coupling (batsale2021biosynthesisandfunctions pages 3-5, batsale2021biosynthesisandfunctions pages 9-10). While the precise functional consequences remain under investigation, KCR1-dependent VLCFA production is essential for maintaining normal membrane homeostasis (batsale2021biosynthesisandfunctions pages 3-5).
| Pathway or process | KCR1 role and evidence | Biological output or consequence | Recent perspective |
|---|---|---|---|
| ER fatty-acid elongation cycle | KCR1 is the shared 3-oxoacyl-CoA reductase of the ER-localized fatty-acid elongase (FAE) complex. After KCS condenses an acyl-CoA with malonyl-CoA, KCR1 reduces the resulting 3-oxoacyl-CoA to 3-hydroxyacyl-CoA using NAD(P)H; PAS2/HCD then dehydrates the product, and CER10/ECR completes the two-carbon elongation cycle (batsale2021biosynthesisandfunctions pages 3-5) | Produces very-long-chain acyl-CoAs used by several membrane, storage, and extracellular-barrier lipid pathways | A 2023 CRISPR-engineered yeast platform reconstituted Arabidopsis FAE complexes containing KCR1, PAS2, CER10, and individual KCS proteins, enabling systematic analysis of KCS-dependent product profiles (batsale2023tacklingfunctionalredundancy pages 12-13, batsale2023tacklingfunctionalredundancy pages 1-2) |
| Chain-length specification | KCR1 accepts a broad range of 3-oxoacyl-CoA elongation intermediates. The associated KCS enzyme principally determines substrate and product chain length, whereas KCR1, HCD, and ECR constitute broadly acting shared machinery (batsale2023tacklingfunctionalredundancy pages 1-2) | Permits multiple KCS-defined FAE complexes to generate the diverse VLCFA chain lengths required throughout the plant | Current models emphasize combinatorial FAE organization, possible KCS homo-/heterodimerization, and partner-dependent activity rather than KCR1-driven chain-length selection (batsale2023tacklingfunctionalredundancy pages 12-13) |
| Cuticular-wax biosynthesis | KCR1 supplies C20–C34 VLCFA precursors that are converted through wax pathways into aldehydes, alkanes, primary and secondary alcohols, ketones, and wax esters (beaudoin2009functionalcharacterizationof pages 1-2, lee2013recentadvancesin pages 1-2) | Supports epicuticular wax crystals and the hydrophobic aerial barrier. Severe KCR1 knockdown reduced stem wax to 11.4% or 3.9% of wild type and produced glossy stems, cuticle permeability, and dehydration sensitivity (beaudoin2009functionalcharacterizationof pages 8-10, beaudoin2009functionalcharacterizationof pages 10-11) | Recent interactome analysis supports organization of KCR with HCD, ECR, PAS1, and accessory proteins such as CER2, potentially coordinating wax-directed elongase activity (xu2023proteininteractomesfor pages 3-4) |
| Sphingolipid formation | KCR1-dependent elongation supplies VLCFAs—commonly C22–C26—for ceramide and complex sphingolipid synthesis. In Arabidopsis, VLCFAs constitute nearly 80% of sphingolipid fatty-acid chains; KCR1 suppression decreases many measured sphingolipid species (beaudoin2009functionalcharacterizationof pages 11-13, batsale2021biosynthesisandfunctions pages 13-14) | Maintains plasma-membrane organization, membrane-domain properties, signaling capacity, and normal development | Current expert interpretation treats KCR1 as a common upstream VLCFA-supply enzyme rather than a sphingolipid-specific catalyst; lipid-class allocation occurs downstream of elongation (batsale2021biosynthesisandfunctions pages 3-5, batsale2021biosynthesisandfunctions pages 5-6) |
| Suberin and cell-wall-associated barriers | KCR1 supplies VLCFA precursors for suberin-associated ω-hydroxy fatty acids, dicarboxylic acids, fatty alcohols, and related compounds. Reduced KCR1 activity lowers longer-chain root fatty acids and causes atypical oxygenated and dicarboxylic products (beaudoin2009functionalcharacterizationof pages 11-13, batsale2021biosynthesisandfunctions pages 3-5) | Contributes to hydrophobic root and periderm barriers governing water loss, solute movement, nutrient homeostasis, and environmental protection | VLCFA-derived suberin is induced by drought, waterlogging, and nematode infection, although these stress responses are established primarily for the pathway and are not all directly demonstrated as KCR1-specific regulation (batsale2021biosynthesisandfunctions pages 13-14) |
| Seed triacylglycerol and root glycerolipids | KCR1 supplies elongated acyl chains incorporated into seed storage lipids and root glycerolipids. Strong knockdown reduced seed-oil VLCFAs by approximately 30% and altered root C20, C22, and C24 fatty acids (beaudoin2009functionalcharacterizationof pages 1-2, beaudoin2009functionalcharacterizationof pages 10-11) | Supports storage-lipid composition, germination-related reserves, and root lipid homeostasis | Reconstituted FAE systems now provide a route to distinguish which KCS–KCR1 combinations generate acyl chains allocated to storage versus structural lipid pools (batsale2023tacklingfunctionalredundancy pages 12-13, batsale2023tacklingfunctionalredundancy pages 1-2) |
| Embryogenesis and morphogenesis | Complete KCR1 loss is embryo lethal and cannot be rescued by KCR2, establishing KCR1 as the essential Arabidopsis microsomal KCR. Partial depletion disrupts several VLCFA-dependent lipid classes simultaneously (beaudoin2009functionalcharacterizationof pages 11-13, beaudoin2009functionalcharacterizationof pages 13-15) | Strong knockdown causes dwarfism, fused or twisted organs, abnormal roots and trichomes, reduced fertility, seed abortion, and severe epidermal defects (beaudoin2009functionalcharacterizationof pages 8-10, beaudoin2009functionalcharacterizationof pages 6-8) | The prevailing interpretation is that these phenotypes reflect combined defects in membrane sphingolipids, cuticular waxes, suberin, and other VLCFA-containing lipids rather than one isolated downstream pathway (batsale2021biosynthesisandfunctions pages 3-5, batsale2021biosynthesisandfunctions pages 5-6) |
| Biotic-stress signaling | Fatty-acid elongation genes, including KCR, can be induced downstream of MYB30 during the hypersensitive response to avirulent bacteria. VLCFA-derived sphingolipids are proposed to participate in defense-associated membrane signaling and programmed cell death (batsale2021biosynthesisandfunctions pages 16-17) | Potentially links VLCFA production to pathogen-triggered signaling, membrane remodeling, and defense responses | The mechanistic link remains incompletely resolved: evidence is stronger for VLCFA and sphingolipid pathways generally than for a unique signaling function of the KCR1 protein itself (batsale2021biosynthesisandfunctions pages 16-17) |
| Abiotic-stress adaptation | Through wax, suberin, sphingolipid, and phospholipid production, KCR1-dependent VLCFA synthesis contributes indirectly to water-barrier function and membrane homeostasis under drought and other environmental stresses (beaudoin2009functionalcharacterizationof pages 1-2, batsale2021biosynthesisandfunctions pages 3-5) | Influences cuticular water loss, root barrier properties, membrane stability, and stress acclimation; strong KCR1 suppression produces dehydration sensitivity (beaudoin2009functionalcharacterizationof pages 8-10, batsale2021biosynthesisandfunctions pages 13-14) | Recent research increasingly frames FAE complexes as modular metabolic assemblies whose partner composition may tune VLCFA outputs under developmental or environmental conditions, but direct 2023–2024 evidence for KCR1-specific stress regulation remains limited (xu2023proteininteractomesfor pages 3-4, batsale2023tacklingfunctionalredundancy pages 1-2) |
| 2024 comparative FAE research | Work on maize showed that KCR homologs can rescue yeast KCR deficiency and that GL2/GL2-LIKE accessory BAHD proteins alter KCS-dependent VLCFA profiles, including production up to C30 in some engineered contexts (alexander2024theimpactof pages 11-12) | Demonstrates the biotechnology potential of manipulating KCR-containing FAE systems to modify VLCFA and wax-precursor production | This is comparative evidence from maize, not direct evidence about Arabidopsis KCR1; it informs general FAE-complex regulation but must not be conflated with AtKCR1-specific function (beaudoin2009functionalcharacterizationof pages 2-4, alexander2024theimpactof pages 11-12) |
Table: Summary of KCR1’s reaction within the ER fatty-acid elongase cycle, its downstream contributions to major VLCFA-containing lipid classes, and associated developmental and stress-related processes. The table distinguishes direct Arabidopsis evidence from recent comparative findings in maize.
Homozygous insertional null mutants of KCR1 are embryo lethal, demonstrating that KCR1-dependent VLCFA synthesis is absolutely required during embryogenesis (beaudoin2009functionalcharacterizationof pages 6-8, beaudoin2009functionalcharacterizationof pages 13-15, beaudoin2009functionalcharacterizationof pages 11-13). Heterozygous kcr1/+ plants show no obvious developmental, VLCFA-composition, or cuticular wax differences from wild type (beaudoin2009functionalcharacterizationof pages 8-10). The embryo lethality cannot be rescued by expression of AtKCR2 under the AtKCR1 promoter, confirming that KCR1 is the unique essential microsomal KCR in Arabidopsis (beaudoin2009functionalcharacterizationof pages 11-13).
RNA interference (RNAi) suppression of KCR1 produces variable phenotypes that correlate with the degree of transcript reduction (beaudoin2009functionalcharacterizationof pages 8-10, beaudoin2009functionalcharacterizationof pages 6-8). Strongly suppressed lines exhibit:
The most visually striking phenotype of strong KCR1 knockdown lines is the glossy appearance of inflorescence stems, which lack the dense epicuticular wax crystals present on wild-type stems, producing a shiny surface (beaudoin2009functionalcharacterizationof pages 10-11, beaudoin2009functionalcharacterizationof pages 13-15). This glossy phenotype reflects severe cuticular wax deficiency: total stem wax levels fell to 11.4% of wild type in one RNAi line and to only 3.9% in another severe line (beaudoin2009functionalcharacterizationof pages 10-11). Reductions occurred across all wax compound classes (beaudoin2009functionalcharacterizationof pages 10-11). In contrast, weaker nonglossy RNAi lines retained 75-80% of wild-type wax levels but still showed modest wax reductions (beaudoin2009functionalcharacterizationof pages 10-11).
The glossy phenotype is associated with defective cuticle formation and dramatically increased cuticle permeability. Glossy seedlings stain completely with toluidine blue, indicating a highly permeable, severely abnormal cuticle, whereas nonglossy lines show milder or patchy cuticular defects (beaudoin2009functionalcharacterizationof pages 8-10, beaudoin2009functionalcharacterizationof pages 10-11). The severity of the glossy appearance directly correlates with the extent of AtKCR1 suppression, diminished VLCFA production, and consequent failure to synthesize normal epicuticular wax and cuticular structures (beaudoin2009functionalcharacterizationof pages 10-11).
KCR1 suppression produces specific alterations in VLCFA-containing lipid classes. In roots, strong knockdown lines show reduced C20, C22, and C24 fatty acids and accumulate atypical dicarboxylic and ω-hydroxylated fatty acids (beaudoin2009functionalcharacterizationof pages 11-13). In seeds, VLCFA content in oil decreases by approximately 30% in severe lines (beaudoin2009functionalcharacterizationof pages 10-11). Sphingolipid analysis reveals moderate but statistically significant decreases in nearly all measured sphingolipid species (beaudoin2009functionalcharacterizationof pages 11-13). These biochemical changes across multiple lipid classes indicate that the pleiotropic developmental phenotypes reflect combined defects in membrane sphingolipids, cuticular waxes, suberin, and other VLCFA-containing lipids rather than impairment of a single isolated downstream pathway (batsale2021biosynthesisandfunctions pages 3-5, batsale2021biosynthesisandfunctions pages 5-6).
A significant methodological advance reported by Batsale et al. (2023) established CRISPR-Cas9-based yeast expression platforms capable of reconstituting different Arabidopsis FAE complexes (batsale2023tacklingfunctionalredundancy pages 12-13, batsale2023tacklingfunctionalredundancy pages 1-2). These engineered strains express Arabidopsis KCR1, PAS2, CER10, and individual KCS proteins, replacing the corresponding yeast genes. Detailed analysis of VLCFAs produced in these yeast systems allows systematic characterization of KCS substrate specificities and provides evidence that weak physical interactions between KCS proteins and the other core subunits do not necessarily prevent catalytic activity (batsale2023tacklingfunctionalredundancy pages 12-13). The platform also enables investigation of KCS homo- and heterodimerization and facilitates exploration of how core enzymes such as KCR1 operate with different KCS isoforms (batsale2023tacklingfunctionalredundancy pages 12-13). Transient expression in Nicotiana benthamiana was additionally used to assess activity and subcellular localization of Arabidopsis FAE components in planta (batsale2023tacklingfunctionalredundancy pages 1-2).
A 2023 review by Xu et al. on protein interactomes for plant lipid biosynthesis synthesized recent findings on FAE complex organization (xu2023proteininteractomesfor pages 3-4). The analysis highlighted BiFC and affinity-purification evidence supporting a core KCR-ECR-HCD complex that associates with the scaffold protein PAS1 and the accessory protein CER2 (xu2023proteininteractomesfor pages 3-4). The review emphasized that FAE complexes function as modular assemblies whose composition may be tuned under different developmental or environmental conditions, although direct evidence for environmentally regulated KCR1-specific complex remodeling remains limited (xu2023proteininteractomesfor pages 3-4).
Alexander et al. (2024) examined maize KCR homologs and BAHD-family accessory proteins in yeast FAE systems (alexander2024theimpactof pages 11-12). The study demonstrated that maize ZmKCR1 and ZmKCR2 can functionally rescue yeast KCR-null mutants and investigated how GL2 and GL2-LIKE proteins modify the VLCFA product profiles of reconstituted complexes, enabling synthesis of VLCFAs up to C30 in some contexts (alexander2024theimpactof pages 11-12). While this work provides insights into general FAE complex regulation and the biotechnology potential of manipulating elongase systems, it represents comparative evidence from maize rather than direct evidence about Arabidopsis KCR1 function and must be interpreted accordingly (beaudoin2009functionalcharacterizationof pages 2-4, alexander2024theimpactof pages 11-12).
Fatty acid elongation genes, including KCR, can be induced downstream of the MYB30 transcription factor during the hypersensitive response to avirulent bacterial pathogens (batsale2021biosynthesisandfunctions pages 16-17). VLCFA-derived sphingolipids have been proposed to participate in defense-associated membrane signaling and programmed cell death, although the precise molecular mechanisms remain incompletely characterized (batsale2021biosynthesisandfunctions pages 16-17). Current evidence is stronger for VLCFA and sphingolipid pathway involvement generally than for a unique signaling function specifically attributable to KCR1 protein (batsale2021biosynthesisandfunctions pages 16-17).
Through its contributions to wax, suberin, sphingolipid, and phospholipid production, KCR1-dependent VLCFA synthesis influences plant responses to drought and other environmental stresses (beaudoin2009functionalcharacterizationof pages 1-2, batsale2021biosynthesisandfunctions pages 3-5, batsale2021biosynthesisandfunctions pages 13-14). The cuticular wax layer limits transpirational water loss, suberin barriers control root water and solute movement, and membrane lipids maintain membrane stability and function under stress conditions (beaudoin2009functionalcharacterizationof pages 1-2, batsale2021biosynthesisandfunctions pages 13-14). Strong KCR1 suppression produces dehydration sensitivity, consistent with compromised cuticle function (beaudoin2009functionalcharacterizationof pages 8-10). Recent research increasingly frames FAE complexes as modular metabolic assemblies whose partner composition may tune VLCFA outputs under developmental or environmental conditions, although direct evidence for stress-regulated KCR1-specific mechanisms from 2023-2024 literature remains limited (xu2023proteininteractomesfor pages 3-4, batsale2023tacklingfunctionalredundancy pages 1-2).
KCR1 (At1g67730) encodes the essential β-ketoacyl-CoA reductase of the Arabidopsis endoplasmic reticulum fatty acid elongase complex. As a 35.7-kDa member of the short-chain dehydrogenase/reductase family, KCR1 catalyzes the NAD(P)H-dependent reduction of 3-oxoacyl-CoA to 3-hydroxyacyl-CoA, the first reduction step in each iterative cycle that extends fatty acids beyond 18 carbons into very-long-chain fatty acids (VLCFAs). Unlike chain-length-selective KCS condensing enzymes, KCR1 exhibits broad substrate specificity and functions as a shared component of multiple FAE complexes that produce the diverse VLCFA chain lengths required throughout the plant.
KCR1 occupies a central position in plant lipid metabolism because its VLCFA products feed multiple downstream pathways, including cuticular wax biosynthesis, sphingolipid formation, seed storage lipids, suberin barriers, and membrane phospholipids. Complete loss of KCR1 is embryo lethal, demonstrating an absolute requirement for VLCFA synthesis during embryogenesis. Partial KCR1 reduction produces severity-dependent phenotypes including the glossy stem phenotype (reflecting severe cuticular wax deficiency), dwarfism, organ fusion, twisted growth, reproductive abnormalities, defective roots and trichomes, and dehydration sensitivity. These pleiotropic effects reflect simultaneous disruption of multiple VLCFA-dependent lipid classes rather than impairment of a single specialized pathway.
Recent advances (2023-2024) include yeast reconstitution platforms that enable systematic dissection of Arabidopsis FAE complex composition and function, protein interactome analyses revealing KCR associations with HCD, ECR, PAS1, and CER2, and comparative studies in maize illuminating accessory protein regulation of elongase activity. These developments support an emerging view of FAE complexes as modular, potentially regulatable assemblies whose composition determines VLCFA output, although many mechanistic details of complex organization and regulation remain to be elucidated.
Primary Functional Characterization:
- Beaudoin et al. (2009). Plant Physiology 150:1174-1191. DOI: 10.1104/pp.109.137497 (beaudoin2009functionalcharacterizationof pages 1-2, beaudoin2009functionalcharacterizationof pages 2-4, beaudoin2009functionalcharacterizationof pages 11-13, beaudoin2009functionalcharacterizationof pages 4-6, beaudoin2009functionalcharacterizationof pages 8-10, beaudoin2009functionalcharacterizationof pages 10-11, beaudoin2009functionalcharacterizationof pages 6-8)
Comprehensive Reviews:
- Batsale et al. (2021). Cells 10:1284. DOI: 10.3390/cells10061284 (batsale2021biosynthesisandfunctions pages 3-5, batsale2021biosynthesisandfunctions pages 5-6, batsale2021biosynthesisandfunctions pages 13-14)
Recent Advances (2023-2024):
- Batsale et al. (2023). Frontiers in Plant Science 14. DOI: 10.3389/fpls.2023.1107333 (batsale2023tacklingfunctionalredundancy pages 1-2, batsale2023tacklingfunctionalredundancy pages 2-3, batsale2023tacklingfunctionalredundancy pages 3-4, batsale2023tacklingfunctionalredundancy pages 12-13)
- Xu et al. (2023). Plant Biotechnology Journal 21:1734-1744. DOI: 10.1111/pbi.14027 (xu2023proteininteractomesfor pages 3-4)
- Alexander et al. (2024). Frontiers in Plant Science 15. DOI: 10.3389/fpls.2024.1403779 (alexander2024theimpactof pages 11-12)
Additional Key Studies:
- Lee & Suh (2013). Molecular Plant 6:246-249. DOI: 10.1093/mp/sss159 (lee2013recentadvancesin pages 1-2)
- Morineau et al. (2016). PLoS ONE 11:e0160631. DOI: 10.1371/journal.pone.0160631 (morineau2016dualfattyacid pages 1-2, morineau2016dualfattyacid pages 11-12)
References
(beaudoin2009functionalcharacterizationof pages 2-4): Frédéric Beaudoin, Xianzhong Wu, Fengling Li, Richard P. Haslam, Jennifer E. Markham, Huanquan Zheng, Johnathan A. Napier, and Ljerka Kunst. Functional characterization of the arabidopsis β -ketoacyl-coenzyme a reductase candidates of the fatty acid elongase. Plant Physiology, 150:1174-1191, May 2009. URL: https://doi.org/10.1104/pp.109.137497, doi:10.1104/pp.109.137497. This article has 328 citations and is from a highest quality peer-reviewed journal.
(beaudoin2009functionalcharacterizationof pages 11-13): Frédéric Beaudoin, Xianzhong Wu, Fengling Li, Richard P. Haslam, Jennifer E. Markham, Huanquan Zheng, Johnathan A. Napier, and Ljerka Kunst. Functional characterization of the arabidopsis β -ketoacyl-coenzyme a reductase candidates of the fatty acid elongase. Plant Physiology, 150:1174-1191, May 2009. URL: https://doi.org/10.1104/pp.109.137497, doi:10.1104/pp.109.137497. This article has 328 citations and is from a highest quality peer-reviewed journal.
(beaudoin2009functionalcharacterizationof pages 1-2): Frédéric Beaudoin, Xianzhong Wu, Fengling Li, Richard P. Haslam, Jennifer E. Markham, Huanquan Zheng, Johnathan A. Napier, and Ljerka Kunst. Functional characterization of the arabidopsis β -ketoacyl-coenzyme a reductase candidates of the fatty acid elongase. Plant Physiology, 150:1174-1191, May 2009. URL: https://doi.org/10.1104/pp.109.137497, doi:10.1104/pp.109.137497. This article has 328 citations and is from a highest quality peer-reviewed journal.
(zheng2019co‐expressionanalysisaids pages 1-4): Jun Zheng, Cheng He, Yang Qin, Guifang Lin, Woojun D. Park, Minghao Sun, Jian Li, Xiaoduo Lu, Chunyi Zhang, Cheng‐Ting Yeh, Chathura J. Gunasekara, Erliang Zeng, Hairong Wei, Patrick S. Schnable, Guoying Wang, and Sanzhen Liu. Co‐expression analysis aids in the identification of genes in the cuticular wax pathway in maize. The Plant Journal, 97:530–542, Dec 2019. URL: https://doi.org/10.1111/tpj.14140, doi:10.1111/tpj.14140. This article has 62 citations.
(batsale2021biosynthesisandfunctions pages 3-5): Marguerite Batsale, Delphine Bahammou, Laetitia Fouillen, Sébastien Mongrand, Jérôme Joubès, and Frédéric Domergue. Biosynthesis and functions of very-long-chain fatty acids in the responses of plants to abiotic and biotic stresses. Cells, 10:1284, May 2021. URL: https://doi.org/10.3390/cells10061284, doi:10.3390/cells10061284. This article has 262 citations.
(batsale2023tacklingfunctionalredundancy pages 1-2): Marguerite Batsale, Marie Alonso, Stéphanie Pascal, Didier Thoraval, Richard P. Haslam, Frédéric Beaudoin, Frédéric Domergue, and Jérôme Joubès. Tackling functional redundancy of arabidopsis fatty acid elongase complexes. Frontiers in Plant Science, Jan 2023. URL: https://doi.org/10.3389/fpls.2023.1107333, doi:10.3389/fpls.2023.1107333. This article has 48 citations.
(lee2013recentadvancesin pages 1-2): Saet Buyl Lee and Mi Chung Suh. Recent advances in cuticular wax biosynthesis and its regulation in arabidopsis. Molecular plant, 6 2:246-9, Mar 2013. URL: https://doi.org/10.1093/mp/sss159, doi:10.1093/mp/sss159. This article has 246 citations and is from a highest quality peer-reviewed journal.
(beaudoin2009functionalcharacterizationof pages 4-6): Frédéric Beaudoin, Xianzhong Wu, Fengling Li, Richard P. Haslam, Jennifer E. Markham, Huanquan Zheng, Johnathan A. Napier, and Ljerka Kunst. Functional characterization of the arabidopsis β -ketoacyl-coenzyme a reductase candidates of the fatty acid elongase. Plant Physiology, 150:1174-1191, May 2009. URL: https://doi.org/10.1104/pp.109.137497, doi:10.1104/pp.109.137497. This article has 328 citations and is from a highest quality peer-reviewed journal.
(batsale2023tacklingfunctionalredundancy pages 3-4): Marguerite Batsale, Marie Alonso, Stéphanie Pascal, Didier Thoraval, Richard P. Haslam, Frédéric Beaudoin, Frédéric Domergue, and Jérôme Joubès. Tackling functional redundancy of arabidopsis fatty acid elongase complexes. Frontiers in Plant Science, Jan 2023. URL: https://doi.org/10.3389/fpls.2023.1107333, doi:10.3389/fpls.2023.1107333. This article has 48 citations.
(xu2023proteininteractomesfor pages 3-4): Yang Xu, Stacy D. Singer, and Guanqun Chen. Protein interactomes for plant lipid biosynthesis and their biotechnological applications. Plant Biotechnology Journal, 21:1734-1744, Mar 2023. URL: https://doi.org/10.1111/pbi.14027, doi:10.1111/pbi.14027. This article has 38 citations and is from a highest quality peer-reviewed journal.
(batsale2021biosynthesisandfunctions pages 5-6): Marguerite Batsale, Delphine Bahammou, Laetitia Fouillen, Sébastien Mongrand, Jérôme Joubès, and Frédéric Domergue. Biosynthesis and functions of very-long-chain fatty acids in the responses of plants to abiotic and biotic stresses. Cells, 10:1284, May 2021. URL: https://doi.org/10.3390/cells10061284, doi:10.3390/cells10061284. This article has 262 citations.
(beaudoin2009functionalcharacterizationof pages 6-8): Frédéric Beaudoin, Xianzhong Wu, Fengling Li, Richard P. Haslam, Jennifer E. Markham, Huanquan Zheng, Johnathan A. Napier, and Ljerka Kunst. Functional characterization of the arabidopsis β -ketoacyl-coenzyme a reductase candidates of the fatty acid elongase. Plant Physiology, 150:1174-1191, May 2009. URL: https://doi.org/10.1104/pp.109.137497, doi:10.1104/pp.109.137497. This article has 328 citations and is from a highest quality peer-reviewed journal.
(beaudoin2009functionalcharacterizationof pages 13-15): Frédéric Beaudoin, Xianzhong Wu, Fengling Li, Richard P. Haslam, Jennifer E. Markham, Huanquan Zheng, Johnathan A. Napier, and Ljerka Kunst. Functional characterization of the arabidopsis β -ketoacyl-coenzyme a reductase candidates of the fatty acid elongase. Plant Physiology, 150:1174-1191, May 2009. URL: https://doi.org/10.1104/pp.109.137497, doi:10.1104/pp.109.137497. This article has 328 citations and is from a highest quality peer-reviewed journal.
(beaudoin2009functionalcharacterizationof pages 8-10): Frédéric Beaudoin, Xianzhong Wu, Fengling Li, Richard P. Haslam, Jennifer E. Markham, Huanquan Zheng, Johnathan A. Napier, and Ljerka Kunst. Functional characterization of the arabidopsis β -ketoacyl-coenzyme a reductase candidates of the fatty acid elongase. Plant Physiology, 150:1174-1191, May 2009. URL: https://doi.org/10.1104/pp.109.137497, doi:10.1104/pp.109.137497. This article has 328 citations and is from a highest quality peer-reviewed journal.
(beaudoin2009functionalcharacterizationof pages 10-11): Frédéric Beaudoin, Xianzhong Wu, Fengling Li, Richard P. Haslam, Jennifer E. Markham, Huanquan Zheng, Johnathan A. Napier, and Ljerka Kunst. Functional characterization of the arabidopsis β -ketoacyl-coenzyme a reductase candidates of the fatty acid elongase. Plant Physiology, 150:1174-1191, May 2009. URL: https://doi.org/10.1104/pp.109.137497, doi:10.1104/pp.109.137497. This article has 328 citations and is from a highest quality peer-reviewed journal.
(batsale2023tacklingfunctionalredundancy pages 2-3): Marguerite Batsale, Marie Alonso, Stéphanie Pascal, Didier Thoraval, Richard P. Haslam, Frédéric Beaudoin, Frédéric Domergue, and Jérôme Joubès. Tackling functional redundancy of arabidopsis fatty acid elongase complexes. Frontiers in Plant Science, Jan 2023. URL: https://doi.org/10.3389/fpls.2023.1107333, doi:10.3389/fpls.2023.1107333. This article has 48 citations.
(batsale2021biosynthesisandfunctions pages 13-14): Marguerite Batsale, Delphine Bahammou, Laetitia Fouillen, Sébastien Mongrand, Jérôme Joubès, and Frédéric Domergue. Biosynthesis and functions of very-long-chain fatty acids in the responses of plants to abiotic and biotic stresses. Cells, 10:1284, May 2021. URL: https://doi.org/10.3390/cells10061284, doi:10.3390/cells10061284. This article has 262 citations.
(batsale2021biosynthesisandfunctions pages 9-10): Marguerite Batsale, Delphine Bahammou, Laetitia Fouillen, Sébastien Mongrand, Jérôme Joubès, and Frédéric Domergue. Biosynthesis and functions of very-long-chain fatty acids in the responses of plants to abiotic and biotic stresses. Cells, 10:1284, May 2021. URL: https://doi.org/10.3390/cells10061284, doi:10.3390/cells10061284. This article has 262 citations.
(batsale2023tacklingfunctionalredundancy pages 12-13): Marguerite Batsale, Marie Alonso, Stéphanie Pascal, Didier Thoraval, Richard P. Haslam, Frédéric Beaudoin, Frédéric Domergue, and Jérôme Joubès. Tackling functional redundancy of arabidopsis fatty acid elongase complexes. Frontiers in Plant Science, Jan 2023. URL: https://doi.org/10.3389/fpls.2023.1107333, doi:10.3389/fpls.2023.1107333. This article has 48 citations.
(batsale2021biosynthesisandfunctions pages 16-17): Marguerite Batsale, Delphine Bahammou, Laetitia Fouillen, Sébastien Mongrand, Jérôme Joubès, and Frédéric Domergue. Biosynthesis and functions of very-long-chain fatty acids in the responses of plants to abiotic and biotic stresses. Cells, 10:1284, May 2021. URL: https://doi.org/10.3390/cells10061284, doi:10.3390/cells10061284. This article has 262 citations.
(alexander2024theimpactof pages 11-12): Liza Esther Alexander, Dirk Winkelman, Kenna E. Stenback, Madison Lane, Katelyn R. Campbell, Elysse Trost, Kayla Flyckt, Michael A. Schelling, Ludmila Rizhsky, Marna D. Yandeau-Nelson, and Basil J. Nikolau. The impact of the glossy2 and glossy2-like bahd-proteins in affecting the product profile of the maize fatty acid elongase. Frontiers in Plant Science, Jul 2024. URL: https://doi.org/10.3389/fpls.2024.1403779, doi:10.3389/fpls.2024.1403779. This article has 6 citations.
(morineau2016dualfattyacid pages 1-2): Céline Morineau, Lionel Gissot, Yannick Bellec, Kian Hematy, Frédérique Tellier, Charlotte Renne, Richard Haslam, Frédéric Beaudoin, Johnathan Napier, and Jean-Denis Faure. Dual fatty acid elongase complex interactions in arabidopsis. PLoS ONE, 11:e0160631, Sep 2016. URL: https://doi.org/10.1371/journal.pone.0160631, doi:10.1371/journal.pone.0160631. This article has 31 citations and is from a peer-reviewed journal.
(morineau2016dualfattyacid pages 11-12): Céline Morineau, Lionel Gissot, Yannick Bellec, Kian Hematy, Frédérique Tellier, Charlotte Renne, Richard Haslam, Frédéric Beaudoin, Johnathan Napier, and Jean-Denis Faure. Dual fatty acid elongase complex interactions in arabidopsis. PLoS ONE, 11:e0160631, Sep 2016. URL: https://doi.org/10.1371/journal.pone.0160631, doi:10.1371/journal.pone.0160631. This article has 31 citations and is from a peer-reviewed journal.