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.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
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.
Target identity (as provided): UniProt B9INH0, Populus trichocarpa, annotated as glutamyl‑tRNA(Gln) amidotransferase subunit C (GatC family), with predicted chloroplastic/mitochondrial localization.
Symbol ambiguity check: The symbol “GATC” is highly ambiguous in biology (e.g., the DNA sequence motif GATC recognized by Dam methylase; bacterial operon gene names). The relevant literature that matches your UniProt description consistently uses GatC to refer to the small accessory subunit of the heterotrimeric GatCAB tRNA‑dependent amidotransferase complex that participates in indirect aminoacylation (tRNA-dependent transamidation). This meaning (GatC) is clearly supported by mechanistic GatCAB literature and plant organellar GatCAB studies, which directly investigate GatA/B/C subunits and their organellar targeting (sheppard2008ontheevolution pages 1-2, pujol2008dualtargetedtrnadependentamidotransferase pages 1-2).
Species-specific evidence limitation: Searches did not retrieve primary experimental papers explicitly naming Populus trichocarpa UniProt B9INH0 (or its ORF name) with biochemical or localization experiments. Therefore, Populus functional annotation must be treated as orthology-/family-based inference, anchored by (i) the conserved GatCAB mechanism, (ii) direct plant evidence from Arabidopsis thaliana, and (iii) recent angiosperm comparative genomics indicating broad retention of organellar GatCAB in photosynthetic plants (pujol2008dualtargetedtrnadependentamidotransferase pages 1-2, detar2024photosyntheticdemandson pages 4-8).
In many organisms, glutaminyl‑tRNA synthetase (GlnRS) is absent from certain compartments (or entirely absent in a lineage). In such systems, Gln-tRNA*Gln* is produced by an indirect two-step pathway:
1. A nondiscriminating glutamyl‑tRNA synthetase (ND-GluRS) misacylates tRNA*Gln* with glutamate to form Glu‑tRNA*Gln*.
2. A tRNA-dependent amidotransferase (AdT), most commonly GatCAB, converts Glu‑tRNA*Gln* into Gln‑tRNA*Gln* by a transamidation reaction (pujol2008dualtargetedtrnadependentamidotransferase pages 1-2, sheppard2008ontheevolution pages 1-2).
Plants (demonstrated in Arabidopsis) use this indirect route in organelles: mitochondrial and chloroplastic Gln‑tRNA*Gln* synthesis is performed by ND‑GluRS followed by GatCAB (pujol2008dualtargetedtrnadependentamidotransferase pages 1-2).
GatCAB-catalyzed transamidation is generally described as a three-step process (mechanistically conserved across systems):
1. ATP-dependent activation (phosphorylation) of the side-chain carboxyl group of the misacylated amino acid attached to tRNA (Glu or Asp).
2. Ammonia generation by hydrolysis of an amide donor (typically glutamine, sometimes asparagine depending on organism/system).
3. Amidation of the activated intermediate using ammonia, yielding the cognate amide aminoacyl‑tRNA product (Gln‑tRNA*Gln* and/or Asn‑tRNA*Asn*) (sheppard2008ontheevolution pages 1-2, sheppard2007thehelicobacterpylori pages 1-2).
Thus, the minimal inputs for GatCAB activity are: misacylated aminoacyl‑tRNA substrate (e.g., Glu‑tRNA*Gln*), ATP, and an amide donor (often glutamine), with the products being correctly amidated aa‑tRNA (e.g., Gln‑tRNA*Gln*), along with ADP/Pi (and glutamate as a byproduct of glutamine hydrolysis) as expected from the described reaction steps (sheppard2008ontheevolution pages 1-2, sheppard2007thehelicobacterpylori pages 1-2).
Mechanistic assignments from conserved biochemical literature:
- GatA provides the glutaminase/amidase activity that hydrolyzes glutamine to generate ammonia. In Helicobacter pylori, mutations in the GatA catalytic triad abolished glutaminase activity and thereby prevented glutamine-dependent transamidation (sheppard2007thehelicobacterpylori pages 1-2).
- GatB (or GatE in GatDE systems) performs the ATP-dependent activation step and is central to the transamidation chemistry on the tRNA-linked substrate (sheppard2008ontheevolution pages 1-2, sheppard2007thehelicobacterpylori pages 1-2).
- GatC is a small accessory subunit. Sheppard & Söll (2008) describe GatC as required for proper folding of GatA and for GatA binding to GatB, i.e., GatC helps assemble and stabilize the functional heterotrimeric complex (sheppard2008ontheevolution pages 1-2). In the plant context, Pujol et al. describe GatC as a structural/linker element that interacts with GatA and GatB via its termini (pujol2008dualtargetedtrnadependentamidotransferase pages 4-5).
Functional implication for Populus B9INH0: The primary role of GatC is therefore best annotated as complex assembly/stability within organellar GatCAB, enabling efficient organellar production of Gln‑tRNA*Gln* (and, depending on compartment and substrate availability, potentially supporting Asn‑tRNA*Asn* formation by the same general pathway) (pujol2008dualtargetedtrnadependentamidotransferase pages 4-5, sheppard2008ontheevolution pages 1-2).
A key plant-specific result is that the GatCAB machinery is dual-targeted:
- In Arabidopsis thaliana, the genes encoding GatA/B/C are nuclear, and each protein has an N-terminal extension consistent with organellar targeting. Pujol et al. (PNAS, Apr 2008, https://doi.org/10.1073/pnas.0712299105) provided in vitro import assays showing that GatA, GatB, and GatC are imported into both mitochondria and chloroplasts and processed to mature, protease-protected forms (pujol2008dualtargetedtrnadependentamidotransferase pages 2-4, pujol2008dualtargetedtrnadependentamidotransferase pages 1-2).
- They also report specific precursor sizes: GatC is 155 aa with an ~60-aa N-terminal extension (precursor) in Arabidopsis, highlighting how substantial targeting sequences can be in plant GatC proteins (pujol2008dualtargetedtrnadependentamidotransferase pages 2-4).
Given that UniProt annotates Populus B9INH0 as chloroplastic/mitochondrial, the most conservative evidence-based interpretation is that Populus GatC is likewise a nuclear-encoded organellar protein functioning in both organelles (supported directly in Arabidopsis and consistent with broader plant trends of dual-targeted translation machinery) (pujol2008dualtargetedtrnadependentamidotransferase pages 1-2, detar2024photosyntheticdemandson pages 1-4).
In plants, GatCAB sits in the organellar translation supply chain, upstream of ribosomal protein synthesis:
- It ensures availability of correctly charged Gln‑tRNA*Gln* in organelles that may not have an organellar GlnRS, by correcting ND‑GluRS misacylation via transamidation (pujol2008dualtargetedtrnadependentamidotransferase pages 1-2).
- Because plastids have high translational demand (photosynthetic complexes), the organellar tRNA metabolism machinery is under strong functional constraint in photosynthetic lineages, shaping its evolutionary retention (detar2024photosyntheticdemandson pages 1-4).
DeTar et al. (PNAS, Oct 2024, preprint DOI shown; https://doi.org/10.1101/2023.08.01.551541) conducted a comparative analysis of organellar/cytosolic translation components across angiosperms (including 7 heterotrophs, 8 hemiparasites, 10 autotrophs). They explicitly frame GatCAB as the “bacterial-type” solution to organellar Gln‑tRNA*Gln* synthesis (GluRS misacylation followed by GatCAB transamidation) and report that most species retain at least some GatCAB subunits, but that extreme heterotrophs (notably Rafflesiaceae) appear to have lost all GatCAB subunits (detar2024photosyntheticdemandson pages 4-8, detar2024photosyntheticdemandson pages 11-15).
This recent work provides a modern evolutionary context for interpreting Populus: as a photosynthetic tree, Populus trichocarpa falls on the side of angiosperms predicted to retain specialized organellar tRNA metabolism, consistent with UniProt’s assignment of a GatC family member (detar2024photosyntheticdemandson pages 4-8, detar2024photosyntheticdemandson pages 1-4).
DeTar et al. propose that some lineages may compensate for loss of organellar GatCAB by retargeting cytosolic enzymes. Specifically, they note that retargeting of cytosolic GlnRS could explain survival after loss of organellar GatCAB in at least one discussed species context (detar2024photosyntheticdemandson pages 8-11). They also provide statistical support for broader retargeting phenomena: cytosolic aaRS are disproportionately retargeted to mitochondria in obligate heterotrophs (p = 0.0341), and there is a strong correlation between organellar aaRS loss and cytosolic enzyme retargeting (p = 0.005) (detar2024photosyntheticdemandson pages 8-11).
Because GatC is a core component of the organellar translation apparatus, its main “applications” are in:
- Plant molecular genetics / organelle biology: manipulating organellar translation components (including GatCAB subunits) is used to test constraints on plastid/mitochondrial translation and how plants respond to organellar mistranslation or translation stress (contextualized by DeTar et al.’s emphasis on photosynthetic demand and by plant-focused GatCAB work) (detar2024photosyntheticdemandson pages 1-4, pujol2008dualtargetedtrnadependentamidotransferase pages 1-2).
- Comparative genomics & annotation pipelines: GatC family/domain assignments (PF02686/IPR003837) are used to annotate organellar translation genes across plant genomes; recent comparative studies explicitly track presence/absence of GatCAB components as indicators of organellar translational system architecture (detar2024photosyntheticdemandson pages 4-8).
(Direct Populus-specific implementations were not retrieved; this section is necessarily framed in terms of general plant/angiosperm use cases consistent with the available evidence.)
Key quantitative/statistical anchors relevant to GatCAB (and by inference GatC):
- Plant GatCAB turnover: Purified Arabidopsis AdT (GatCAB) reported kcat ≈ 3 s⁻¹ on a Thermus thermophilus substrate, within the range of bacterial enzymes (Pujol et al., PNAS, Apr 2008, https://doi.org/10.1073/pnas.0712299105) (pujol2008dualtargetedtrnadependentamidotransferase pages 2-2).
- Plant GatC targeting extension: Arabidopsis GatC precursor length 155 aa with ~60-aa N-terminal targeting extension (pujol2008dualtargetedtrnadependentamidotransferase pages 2-4).
- Well-characterized homolog kinetics and donor preference: H. pylori GatCAB kcat/Km 1368.4 and 3059.3 s⁻¹/mM for Asp‑tRNA*Asn* and Glu‑tRNA*Gln*, respectively; glutaminase activation ~22-fold by Asp‑tRNA*Asn* + ATP; 129-fold preference for glutamine over asparagine as amide donor (Sheppard et al., JBC, Apr 2007, https://doi.org/10.1074/jbc.m700398200) (sheppard2007thehelicobacterpylori pages 1-2).
- 2024 angiosperm survey statistics: dataset sizes (7 heterotrophs/8 hemiparasites/10 autotrophs) and retargeting statistics (p = 0.0341 for mitochondrial retargeting enrichment in heterotrophs; p = 0.005 correlation between organellar aaRS loss and cytosolic retargeting) (DeTar et al., PNAS, Oct 2024, https://doi.org/10.1101/2023.08.01.551541) (detar2024photosyntheticdemandson pages 8-11, detar2024photosyntheticdemandson pages 4-8).
Most supported primary function (Populus inference): B9INH0 encodes GatC, the accessory/structural subunit of the organellar GatCAB tRNA-dependent amidotransferase complex. GatC’s primary role is to support assembly/stability of GatCAB (including GatA folding and GatA–GatB association), thereby enabling the conserved ATP- and glutamine-dependent transamidation pathway that generates Gln‑tRNA*Gln* from Glu‑tRNA*Gln* in organelles (sheppard2008ontheevolution pages 1-2, pujol2008dualtargetedtrnadependentamidotransferase pages 4-5).
Likely localization (Populus inference, with direct plant support): Mitochondria and chloroplasts, based on strong Arabidopsis import evidence for GatA/B/C and broad prevalence of dual-targeted organellar translation proteins in plants; this matches UniProt’s chloroplastic/mitochondrial annotation for B9INH0 (pujol2008dualtargetedtrnadependentamidotransferase pages 2-4, pujol2008dualtargetedtrnadependentamidotransferase pages 1-2, detar2024photosyntheticdemandson pages 1-4).
Pathway: organellar translation—specifically, ensuring the supply of correctly amidated Gln‑tRNA*Gln* to organellar ribosomes in the absence (or limited use) of organellar GlnRS (pujol2008dualtargetedtrnadependentamidotransferase pages 1-2, detar2024photosyntheticdemandson pages 4-8).
| Claim | Evidence details (include numbers) | Organism/system | Source (author year journal) | URL | Publication date | Notes/limitations |
|---|---|---|---|---|---|---|
| Plant organelles synthesize Gln-tRNAGln by an indirect transamidation pathway rather than direct GlnRS charging | In plants, a nondiscriminating GluRS first forms Glu-tRNAGln, which GatCAB then converts to Gln-tRNAGln; Pujol et al. directly assayed transamidation of [14C]Glu-tRNAGln to [14C]Gln-tRNAGln in organellar extracts and purified enzyme (pujol2008dualtargetedtrnadependentamidotransferase pages 2-2, pujol2008dualtargetedtrnadependentamidotransferase pages 2-4, pujol2008dualtargetedtrnadependentamidotransferase pages 1-2) | Arabidopsis organelles; broader plant organelles | Pujol et al. 2008 PNAS | https://doi.org/10.1073/pnas.0712299105 | Apr 2008 | Direct experimental evidence is from Arabidopsis; Populus-specific assay data were not retrieved |
| GatCAB catalysis proceeds through ATP-dependent activation, ammonia generation, and amidation | Reviews and mechanistic studies describe a 3-step reaction: (1) ATP-dependent phosphorylation of the side-chain carboxyl of misacylated Glu/Asp on tRNA, (2) glutamine/asparagine hydrolysis to liberate ammonia, (3) amidation of the activated intermediate to form Gln-tRNAGln or Asn-tRNAAsn (sheppard2008ontheevolution pages 1-2, sheppard2007thehelicobacterpylori pages 1-2) | Bacterial/archaeal/organellar GatCAB systems | Sheppard & Söll 2008 J Mol Biol; Sheppard et al. 2007 J Biol Chem | https://doi.org/10.1016/j.jmb.2008.01.016; https://doi.org/10.1074/jbc.m700398200 | Mar 2008; Apr 2007 | Mechanistic assignment is highly conserved and widely used for plant functional inference, but not measured directly for Populus B9INH0 |
| GatA is the glutaminase subunit | GatA contains the amidase/glutaminase active site; mutating the catalytic triad abolished glutaminase activity and glutamine-dependent amidotransferase activity in H. pylori GatCAB (sheppard2007thehelicobacterpylori pages 1-2) | H. pylori GatCAB; conserved inference for plant GatCAB | Sheppard et al. 2007 J Biol Chem | https://doi.org/10.1074/jbc.m700398200 | Apr 2007 | Subunit role is experimentally defined outside plants but is the accepted annotation basis for plant orthologs |
| GatB is the transamidase/kinase-like catalytic subunit that activates the misacylated tRNA substrate | GatB (or GatE in GatDE systems) performs the ATP-dependent activation/phosphorylation of the attached Glu/Asp and participates in amidation of the activated intermediate (sheppard2008ontheevolution pages 1-2, sheppard2007thehelicobacterpylori pages 1-2) | Bacterial/archaeal/organellar GatCAB systems | Sheppard & Söll 2008 J Mol Biol; Sheppard et al. 2007 J Biol Chem | https://doi.org/10.1016/j.jmb.2008.01.016; https://doi.org/10.1074/jbc.m700398200 | Mar 2008; Apr 2007 | Strong conserved biochemistry; no Populus-specific catalytic dissection retrieved |
| GatC is a small accessory/structural subunit rather than the main catalytic center | GatC is ~100 aa in many bacteria and is required for proper folding of GatA and for GatA binding to GatB; in plant GatCAB, GatC is described as a linker/structural subunit interacting with GatA and GatB via its termini (pujol2008dualtargetedtrnadependentamidotransferase pages 4-5, sheppard2008ontheevolution pages 1-2) | Conserved GatCAB; Arabidopsis plant organelles | Pujol et al. 2008 PNAS; Sheppard & Söll 2008 J Mol Biol | https://doi.org/10.1073/pnas.0712299105; https://doi.org/10.1016/j.jmb.2008.01.016 | Apr 2008; Mar 2008 | This is the most relevant function for Populus GatC B9INH0; direct Populus biochemistry was not found |
| Arabidopsis GatA, GatB, and GatC are dual targeted to both mitochondria and chloroplasts | All three subunits have N-terminal organellar targeting extensions and were imported in vitro into isolated mitochondria and chloroplasts; mature, protease-protected processed forms were observed, and import was inhibited by valinomycin or dark treatment controls (pujol2008dualtargetedtrnadependentamidotransferase pages 2-2, pujol2008dualtargetedtrnadependentamidotransferase pages 2-4, pujol2008dualtargetedtrnadependentamidotransferase pages 1-2) | Arabidopsis thaliana | Pujol et al. 2008 PNAS | https://doi.org/10.1073/pnas.0712299105 | Apr 2008 | Best direct evidence for plant localization; Populus localization remains inferred from orthology/UniProt annotation |
| Plant GatCAB is a shared organellar machinery used in both chloroplasts and mitochondria | The same three Gat subunits, together with a dual-targeted nondiscriminating GluRS, are reported to be shared between mitochondria and chloroplasts for Gln-tRNAGln production (pujol2008dualtargetedtrnadependentamidotransferase pages 1-2) | Arabidopsis thaliana | Pujol et al. 2008 PNAS | https://doi.org/10.1073/pnas.0712299105 | Apr 2008 | Supports UniProt annotation of B9INH0 as chloroplastic/mitochondrial |
| Quantitative plant enzyme activity is consistent with bacterial-type GatCAB amidotransferases | Purified Arabidopsis AdT showed catalytic efficiency in the bacterial range, with reported kcat ≈ 3 s-1 on a Thermus thermophilus substrate (pujol2008dualtargetedtrnadependentamidotransferase pages 2-2) | Arabidopsis enzyme tested with heterologous substrate | Pujol et al. 2008 PNAS | https://doi.org/10.1073/pnas.0712299105 | Apr 2008 | Useful quantitative anchor for plant organellar GatCAB, but not GatC-alone kinetics |
| Quantitative catalytic parameters from a well-characterized homolog support conserved GatCAB function | H. pylori GatCAB transamidated Asp-tRNAAsn and Glu-tRNAGln with kcat/Km values of 1368.4 and 3059.3 s-1/mM, respectively; glutaminase activity was enhanced ~22-fold by Asp-tRNAAsn + ATP; glutamine was used 129-fold more efficiently than asparagine as amide donor (sheppard2007thehelicobacterpylori pages 1-2) | H. pylori | Sheppard et al. 2007 J Biol Chem | https://doi.org/10.1074/jbc.m700398200 | Apr 2007 | Non-plant data, but among the most quantitative available for conserved GatCAB biochemistry |
| Arabidopsis Gat subunits include substantial N-terminal targeting extensions | Reported precursor lengths/extensions: GatA 537 aa with 45-aa extension, GatB 550 aa with 55-aa extension, GatC 155 aa with 60-aa extension (pujol2008dualtargetedtrnadependentamidotransferase pages 2-4) | Arabidopsis thaliana | Pujol et al. 2008 PNAS | https://doi.org/10.1073/pnas.0712299105 | Apr 2008 | Especially relevant to GatC annotation because organellar targeting is a key feature of plant homologs |
| Experimental assay conditions for plant AdT demonstrate direct organellar amidation capacity | Pujol et al. used 100 pmol [14C]Asp-tRNA or 10 pmol [14C]Glu-tRNA with purified Arabidopsis AdT or 15 μg organellar extract, incubated 15 min at 37°C; purification yielded 70 mg pure enzyme from 40 g cells and ~60% pure tRNA (~30× enrichment) (pujol2008dualtargetedtrnadependentamidotransferase pages 4-5) | Arabidopsis thaliana | Pujol et al. 2008 PNAS | https://doi.org/10.1073/pnas.0712299105 | Apr 2008 | Method-level numbers support robustness of the plant functional evidence |
| Recent angiosperm comparative work shows GatCAB is broadly retained but can be lost in extreme heterotrophs | In a 2024 angiosperm survey (7 heterotrophs, 8 hemiparasites, 10 autotrophs), most species retained at least some GatCAB subunits, but Rafflesiaceae appear to have lost all GatCAB subunits; loss is discussed as part of reductive evolution in nonphotosynthetic lineages (detar2024photosyntheticdemandson pages 4-8, detar2024photosyntheticdemandson pages 11-15) | Broad angiosperm comparative dataset | DeTar et al. 2024 PNAS | https://doi.org/10.1101/2023.08.01.551541 | Oct 2024 | Important recent context for conservation of plant organellar GatCAB; not Populus-specific |
| Loss of organellar GatCAB may be compensated by retargeting of cytosolic enzymes in some angiosperms | DeTar et al. propose that retargeting of cytosolic GlnRS could compensate for loss of organellar GatCAB in some species; cytosolic aaRS retargeting to mitochondria was significant (p = 0.0341), with a strong correlation between organellar aaRS loss and cytosolic retargeting (p = 0.005) (detar2024photosyntheticdemandson pages 8-11) | Heterotrophic angiosperms | DeTar et al. 2024 PNAS | https://doi.org/10.1101/2023.08.01.551541 | Oct 2024 | This is evolutionary/compensatory inference, not direct evidence for Populus, which is a photosynthetic tree expected to retain the canonical organellar pathway |
| Populus trichocarpa B9INH0 is best annotated by conserved family/domain evidence rather than direct species-specific experiments | No Populus-specific primary study for POPTRDRAFT_577906 was retrieved; annotation is instead supported by its assignment to the GatC family and by strong Arabidopsis and conserved GatCAB literature showing organellar GatC as the structural subunit of dual-targeted GatCAB (pujol2008dualtargetedtrnadependentamidotransferase pages 2-4, pujol2008dualtargetedtrnadependentamidotransferase pages 4-5, sheppard2008ontheevolution pages 1-2, pujol2008dualtargetedtrnadependentamidotransferase pages 1-2) | Populus trichocarpa inferred from orthology/family | Evidence integrated from Pujol et al. 2008 PNAS; Sheppard & Söll 2008 J Mol Biol | https://doi.org/10.1073/pnas.0712299105; https://doi.org/10.1016/j.jmb.2008.01.016 | Apr 2008; Mar 2008 | Explicitly distinguishes direct evidence from inference, which is important because the symbol GATC can be ambiguous in other contexts |
Table: This table summarizes the strongest available evidence for functional annotation of plant organellar GatC, emphasizing what is directly demonstrated in Arabidopsis and broader conserved GatCAB biochemistry, while clearly marking where Populus trichocarpa annotation is inferred from orthology and family/domain evidence.
References
(sheppard2008ontheevolution pages 1-2): Kelly Sheppard and Dieter Söll. On the evolution of the trna-dependent amidotransferases, gatcab and gatde. Journal of molecular biology, 377 3:831-44, Mar 2008. URL: https://doi.org/10.1016/j.jmb.2008.01.016, doi:10.1016/j.jmb.2008.01.016. This article has 77 citations and is from a domain leading peer-reviewed journal.
(pujol2008dualtargetedtrnadependentamidotransferase pages 1-2): Claire Pujol, Marc Bailly, Daniel Kern, Laurence Maréchal-Drouard, Hubert Becker, and Anne-Marie Duchêne. Dual-targeted trna-dependent amidotransferase ensures both mitochondrial and chloroplastic gln-trnagln synthesis in plants. Proceedings of the National Academy of Sciences, 105:6481-6485, Apr 2008. URL: https://doi.org/10.1073/pnas.0712299105, doi:10.1073/pnas.0712299105. This article has 79 citations and is from a highest quality peer-reviewed journal.
(detar2024photosyntheticdemandson pages 4-8): Rachael Ann DeTar, Joanna Chustecki, Anna Martinez-Hottovy, Luis Federico Ceriotti, Amanda K. Broz, M. Virginia Sanchez-Puerta, Christian Elowsky, Alan C. Christensen, and Daniel B. Sloan. Photosynthetic demands on translational machinery drive retention of redundant trna metabolism in plant organelles. Proceedings of the National Academy of Sciences of the United States of America, Oct 2024. URL: https://doi.org/10.1101/2023.08.01.551541, doi:10.1101/2023.08.01.551541. This article has 2 citations and is from a highest quality peer-reviewed journal.
(sheppard2007thehelicobacterpylori pages 1-2): Kelly Sheppard, Pierre-Marie Akochy, Juan C. Salazar, and Dieter Söll. The helicobacter pylori amidotransferase gatcab is equally efficient in glutamine-dependent transamidation of asp-trnaasn and glu-trnagln*. Journal of Biological Chemistry, 282:11866-11873, Apr 2007. URL: https://doi.org/10.1074/jbc.m700398200, doi:10.1074/jbc.m700398200. This article has 73 citations and is from a domain leading peer-reviewed journal.
(pujol2008dualtargetedtrnadependentamidotransferase pages 4-5): Claire Pujol, Marc Bailly, Daniel Kern, Laurence Maréchal-Drouard, Hubert Becker, and Anne-Marie Duchêne. Dual-targeted trna-dependent amidotransferase ensures both mitochondrial and chloroplastic gln-trnagln synthesis in plants. Proceedings of the National Academy of Sciences, 105:6481-6485, Apr 2008. URL: https://doi.org/10.1073/pnas.0712299105, doi:10.1073/pnas.0712299105. This article has 79 citations and is from a highest quality peer-reviewed journal.
(pujol2008dualtargetedtrnadependentamidotransferase pages 2-4): Claire Pujol, Marc Bailly, Daniel Kern, Laurence Maréchal-Drouard, Hubert Becker, and Anne-Marie Duchêne. Dual-targeted trna-dependent amidotransferase ensures both mitochondrial and chloroplastic gln-trnagln synthesis in plants. Proceedings of the National Academy of Sciences, 105:6481-6485, Apr 2008. URL: https://doi.org/10.1073/pnas.0712299105, doi:10.1073/pnas.0712299105. This article has 79 citations and is from a highest quality peer-reviewed journal.
(detar2024photosyntheticdemandson pages 1-4): Rachael Ann DeTar, Joanna Chustecki, Anna Martinez-Hottovy, Luis Federico Ceriotti, Amanda K. Broz, M. Virginia Sanchez-Puerta, Christian Elowsky, Alan C. Christensen, and Daniel B. Sloan. Photosynthetic demands on translational machinery drive retention of redundant trna metabolism in plant organelles. Proceedings of the National Academy of Sciences of the United States of America, Oct 2024. URL: https://doi.org/10.1101/2023.08.01.551541, doi:10.1101/2023.08.01.551541. This article has 2 citations and is from a highest quality peer-reviewed journal.
(detar2024photosyntheticdemandson pages 11-15): Rachael Ann DeTar, Joanna Chustecki, Anna Martinez-Hottovy, Luis Federico Ceriotti, Amanda K. Broz, M. Virginia Sanchez-Puerta, Christian Elowsky, Alan C. Christensen, and Daniel B. Sloan. Photosynthetic demands on translational machinery drive retention of redundant trna metabolism in plant organelles. Proceedings of the National Academy of Sciences of the United States of America, Oct 2024. URL: https://doi.org/10.1101/2023.08.01.551541, doi:10.1101/2023.08.01.551541. This article has 2 citations and is from a highest quality peer-reviewed journal.
(detar2024photosyntheticdemandson pages 8-11): Rachael Ann DeTar, Joanna Chustecki, Anna Martinez-Hottovy, Luis Federico Ceriotti, Amanda K. Broz, M. Virginia Sanchez-Puerta, Christian Elowsky, Alan C. Christensen, and Daniel B. Sloan. Photosynthetic demands on translational machinery drive retention of redundant trna metabolism in plant organelles. Proceedings of the National Academy of Sciences of the United States of America, Oct 2024. URL: https://doi.org/10.1101/2023.08.01.551541, doi:10.1101/2023.08.01.551541. This article has 2 citations and is from a highest quality peer-reviewed journal.
(pujol2008dualtargetedtrnadependentamidotransferase pages 2-2): Claire Pujol, Marc Bailly, Daniel Kern, Laurence Maréchal-Drouard, Hubert Becker, and Anne-Marie Duchêne. Dual-targeted trna-dependent amidotransferase ensures both mitochondrial and chloroplastic gln-trnagln synthesis in plants. Proceedings of the National Academy of Sciences, 105:6481-6485, Apr 2008. URL: https://doi.org/10.1073/pnas.0712299105, doi:10.1073/pnas.0712299105. This article has 79 citations and is from a highest quality peer-reviewed journal.