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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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.
The UniProt accession C5B1I1 is annotated as a TonB-dependent siderophore receptor protein from Methylorubrum extorquens AM1 and contains canonical TonB-dependent transporter (TBDT) domains (plug domain + TonB-dependent receptor β-barrel) consistent with an outer-membrane, TonB/ExbB/ExbD-coupled uptake receptor for scarce extracellular nutrients (classically ferric-siderophore complexes, but TBDTs can also transport other micronutrients). Mechanistically, TBDTs are 22-strand β-barrel proteins occluded by a plug domain and energized by the TonB–ExbB–ExbD system via a conserved TonB box to open the pore for substrate translocation into the periplasm (Braun 2024) (braun2024substrateuptakeby pages 1-2, braun2024substrateuptakeby pages 2-4, braun2024substrateuptakeby pages 4-6).
Critical identity verification outcome: across the accessible primary literature for M. extorquens AM1 lanthanide/metal uptake, the gene symbol “mluA” is not explicitly linked to a characterized AM1 TonB-dependent receptor (e.g., LutH) or to the lut cluster. Instead, AM1’s best-characterized TonB-dependent receptor for metal uptake is LutH (lanthanide uptake), which is distinct from the UniProt description “siderophore receptor” and is encoded in the AM1 lut locus (MexAM1_META1p1778–p1787). Therefore, the symbol mluA should be treated as ambiguous/under-documented for C5B1I1 in the current literature corpus, and functional annotation should be grounded primarily in (i) the TonB-dependent receptor family mechanism and (ii) AM1 metal-uptake paradigms where relevant, without claiming a specific ligand unless experimentally supported (roszczenkojasinska2020geneproductsand pages 6-7, roszczenkojasinska2020geneproductsand pages 7-10).
Definition and architecture. TBDTs are outer-membrane β-barrel transport proteins whose lumen is blocked by an internal plug domain; they mediate uptake of substrates “too large or too scarce” for diffusion through porins and are powered by the TonB energy transduction system (braun2024substrateuptakeby pages 1-2). A conserved five-residue TonB box in the transporter N-terminus is the main binding site for TonB (braun2024substrateuptakeby pages 1-2).
Energy coupling. Transport is energized by the proton motive force across the inner membrane, transmitted via ExbB–ExbD to TonB. A recurring structural stoichiometry from cryo-EM is ExbB_5–ExbD_2, where five ExbB subunits form a pore enclosing an ExbD dimer (braun2024substrateuptakeby pages 14-15, braun2024substrateuptakeby pages 1-2). Energized TonB interacts with the TonB box and induces plug movement/unfolding to open a channel and allow substrate passage into the periplasm (braun2024substrateuptakeby pages 1-2, celia2026advancesinunderstanding pages 8-9).
Substrate classes and ligand specificity. TBDTs are best known for ferric-siderophore and vitamin B_12 uptake, but the family supports a broad substrate range (braun2024substrateuptakeby pages 1-2). Without substrate-bound structures, uptake assays, or genetics for the specific receptor, ligand specificity cannot be assigned confidently.
While UniProt describes C5B1I1 as a “siderophore receptor,” the best experimentally defined metal-uptake TBDT system in M. extorquens AM1 concerns lanthanide (Ln) uptake via the lut pathway. This system provides a mechanistic template for how TBDTs participate in metal-chelate uptake in methylotrophs:
These data support a general inference relevant to C5B1I1: in methylotrophs, TBDTs frequently function in metal acquisition by importing chelated metal complexes to the periplasm for downstream periplasmic trafficking and/or cytoplasmic import (daumann2022aperspectiveon pages 5-8).
Given the absence of explicit mapping between the gene symbol mluA and C5B1I1 in the retrieved primary literature corpus, the most defensible statement is:
“The gene symbol mluA is ambiguous or literature is limited for this specific protein in Methylorubrum extorquens AM1; thus, functional annotation for UniProt C5B1I1 should be based on its TonB-dependent receptor family/domain architecture and general Gram-negative TBDT mechanisms, rather than assuming it corresponds to LutH or other named AM1 receptors.” (roszczenkojasinska2020geneproductsand pages 6-7, roszczenkojasinska2020geneproductsand pages 7-10)
Outer-membrane active uptake receptor. Based on domain/family assignment as a TonB-dependent receptor and the established mechanism of TBDTs, C5B1I1 most likely functions as an outer-membrane receptor/transporter that binds an extracellular ligand (often a metal-chelate, e.g., ferric-siderophore) and—when energized by TonB—translocates it into the periplasm (braun2024substrateuptakeby pages 1-2, braun2024substrateuptakeby pages 2-4).
Energy transduction dependency. Functionally, this implies dependency on the TonB–ExbB–ExbD system for transport, with ExbB_5–ExbD_2 serving as an inner-membrane motor that relays proton motive force to TonB (braun2024substrateuptakeby pages 14-15, braun2024substrateuptakeby pages 1-2).
Known at the family level: TBDTs can mediate uptake of Fe(III)-siderophores and other micronutrients, with binding sites formed by extracellular loops and plug/barrel interfaces (braun2024substrateuptakeby pages 4-6).
Unknown for C5B1I1 specifically: there is no locus-specific genetic/biochemical evidence in the retrieved corpus identifying the precise ligand for UniProt C5B1I1 in AM1. Therefore, the substrate should be reported as “unknown; predicted siderophore/metal-chelate” unless validated experimentally.
Relevant methylotroph precedent: methylotrophs use related TBDTs (e.g., LutH) in uptake of lanthanide complexes, suggesting that metal-chelate uptake by TBDTs is biologically central in this clade (roszczenkojasinska2020geneproductsand pages 7-10, daumann2022aperspectiveon pages 5-8).
Outer membrane: TBDTs are outer-membrane β-barrel proteins by definition (braun2024substrateuptakeby pages 1-2, braun2024substrateuptakeby pages 2-4). Thus C5B1I1 should be localized to the outer membrane, with extracellular loops exposed externally and a periplasmic TonB box interface.
Periplasmic destination of transported ligand: canonical TBDT transport delivers substrate to the periplasm, from which periplasmic binding proteins and inner-membrane ABC transporters can traffic cargo into the cytoplasm (braun2024substrateuptakeby pages 1-2, roszczenkojasinska2020geneproductsand pages 7-10, daumann2022aperspectiveon pages 5-8).
A key AM1 pathway connecting metal uptake to metabolism is the lanthanide switch, regulating methanol dehydrogenases. AM1 uses a lanthanide-dependent periplasmic methanol dehydrogenase (XoxF1), and lanthanide availability controls expression of mxa vs xox systems; uptake into cells is mediated by a TonB/ABC-linked pathway and is subject to repression under excess metal (roszczenkojasinska2020geneproductsand pages 1-4, roszczenkojasinska2020geneproductsand pages 7-10). In AM1, lanthanides can be transported to the cytoplasm and stored as cytoplasmic inclusions resembling polyphosphate granules, including crystalline lanthanum–phosphate deposits observed by TEM/EDS (roszczenkojasinska2020geneproductsand pages 10-11, roszczenkojasinska2019lanthanidetransportstorage pages 1-5).
Although C5B1I1 is not shown to be LutH, these results establish that AM1 couples TonB-dependent outer-membrane transport to downstream periplasmic/cytoplasmic metal handling.
A 2024 mechanistic review summarizes the current structural model for TonB-dependent transport: plug-occluded β-barrels, TonB-box recognition, and ExbB_5–ExbD_2 stoichiometry mediating pmf-driven force transmission to open TBDTs for periplasmic import (braun2024substrateuptakeby pages 14-15, braun2024substrateuptakeby pages 1-2). This provides the most current authoritative framework for describing C5B1I1’s expected mechanism.
Shiina et al. (2023) identified a TonB-dependent receptor in Methylosinus trichosporium OB3b required for XoxF1 induction in the presence of lanthanides and showed that citrate can strengthen the switch, reinforcing the idea that TonB-dependent receptors are causal components of lanthanide-responsive regulation (shiina2023identificationofa pages 2-5). While not AM1, this is recent primary evidence for TonB receptor function in methylotroph metal switching.
AM1’s lanthanide uptake and mineral storage capacity has been explicitly framed as a basis for developing sustainable recovery of critical metals from “mining leachate, coal fly ash, and postconsumer electronics” (roszczenkojasinska2019lanthanidetransportstorage pages 1-5). Complementary work highlights RH AL1 as a candidate for environmentally friendly biorecovery and links such uptake to TonB-ABC transport systems including the lut cluster (wegner2021extracellularandintracellular pages 1-2).
A 2022 authoritative review describes emerging implementations: development of methylotroph strains/variants for gadolinium capture from medical waste streams and contaminated waters, and the repurposing of lanmodulin for biosensing and green separation (e.g., immobilized LanM sorbents) (daumann2022aperspectiveon pages 15-19). These approaches depend on biological metal binding/uptake traits that include TonB-dependent receptors and metallophore/lanthanophore systems (daumann2022aperspectiveon pages 11-15, zytnick2022discoveryandcharacterization pages 1-3).
Key quantitative values from recent and organism-relevant studies include:
* ExbB_5–ExbD_2 stoichiometry for the inner-membrane motor complex energizing TonB-dependent transport (braun2024substrateuptakeby pages 14-15, braun2024substrateuptakeby pages 1-2).
* AM1 lanthanide switch reporter outputs (RFU/OD_600): in MeOH without La(3+), mxa 323 ± 63 and xox1 44 ± 3; in MeOH + La(3+), mxa 61 ± 10 and xox1 206 ± 11 (roszczenkojasinska2020geneproductsand pages 7-10).
* AM1 mxaF lutH acclimation timeframe and growth: acclimation in ~90–120 h; growth rate 0.14 ± 0.02 h⁻¹ after acclimation (roszczenkojasinska2020geneproductsand pages 7-10).
* Cytoplasmic lanthanum–phosphate storage composition (TEM/EDS): La 22.2 wt%, P 15.1 wt%, O 51.1 wt% in crystalline cytoplasmic deposits (roszczenkojasinska2020geneproductsand pages 10-11).
* In OB3b, lanthanide switch perturbation conditions: 25 mM Ce and 50 mM citrate; ~3-fold reduction of MxaF in wild type under cerium (shiina2023identificationofa pages 2-5).
| Topic | Key finding | Quantitative/statistical data (if any) | Source (author, year) | URL | Citation ID |
|---|---|---|---|---|---|
| Ln uptake model in M. extorquens AM1 | The AM1 lut cluster encodes a proposed lanthanide uptake pathway in which LutH functions as the outer-membrane TonB-dependent receptor, LutA as a periplasmic binding/shuttling protein, and LutE/LutF as the inner-membrane ABC transporter for cytoplasmic import. | Cluster spans MexAM1_META1p1778–p1787; assays reported under 2 μM LaCl3. | Roszczenko-Jasińska et al., 2020 | https://doi.org/10.1038/s41598-020-69401-4 | (roszczenkojasinska2020geneproductsand pages 7-10) |
| lut cluster visualization/model | Figure 4 provides a concise visual summary of the functional annotation: panel (a) maps the lut genes, panel (b) diagrams Ln uptake across the outer membrane/periplasm/cytoplasmic membrane, and panel (c) links genotype to growth phenotype. | Genomic map for MexAM1_META1p1778–p1787; includes lutH in the modeled pathway. | Roszczenko-Jasińska et al., 2020, Figure 4 | https://doi.org/10.1038/s41598-020-69401-4 | (roszczenkojasinska2020geneproductsand media 5258917a) |
| Regulation / lanthanide switch in AM1 | Excess lanthanides repress expression of the TonB-dependent receptor gene and shift transcription from the Ca-dependent mxa system toward xox expression, linking outer-membrane uptake to methanol dehydrogenase remodeling. | WT reporter values in MeOH: mxa 323 ± 63 RFU/OD600 and xox1 44 ± 3; in MeOH + La3+: mxa 61 ± 10 and xox1 206 ± 11. | Roszczenko-Jasińska et al., 2020 | https://doi.org/10.1038/s41598-020-69401-4 | (roszczenkojasinska2020geneproductsand pages 1-4, roszczenkojasinska2020geneproductsand pages 7-10) |
| Alternative uptake / acclimation in AM1 | Even without LutH, AM1 can eventually acclimate and restore Ln-responsive growth/signaling, implying an alternative or slower outer-membrane entry route besides the canonical TonB receptor. | mxaF lutH acclimation occurred after ~90–120 h; acclimated growth rate 0.14 ± 0.02 h⁻¹. | Roszczenko-Jasińska et al., 2020 | https://doi.org/10.1038/s41598-020-69401-4 | (roszczenkojasinska2020geneproductsand pages 7-10) |
| Ln chelator supporting uptake | Methylolanthanin was identified as a biological lanthanide chelator in M. extorquens AM1; its production is required for normal Ln accumulation, supporting the idea that TonB receptors likely recognize a chelated Ln species rather than free ion alone. | Phyllosphere Ln concentrations cited as 0.7–7 μg/g dry weight; experiments used NdCl3 and Nd2O3 to probe low-solubility Ln responses. | Zytnick et al., 2022 | https://doi.org/10.1101/2022.01.19.476857 | (zytnick2022discoveryandcharacterization pages 1-3) |
| Homologous TonB receptor in methanotrophs | In Methylosinus trichosporium OB3b, a TonB-dependent receptor homologous to AM1 LutH is required for proper Ln-dependent MDH switching, strengthening family-level functional inference for LutH-like receptors in methylotrophs. | 25 mM Ce induced XoxF1; 50 mM citrate strengthened the switch; MxaF decreased by ~3-fold in WT. | Shiina et al., 2023 | https://doi.org/10.1128/aem.01413-22 | (shiina2023identificationofa pages 2-5) |
| LanA precedent from another methylotroph | In Methylotuvimicrobium buryatense 5GB1C, mutagenesis identified LanA, a TonB-dependent receptor required for the lanthanide switch; this established TBDRs as causal regulators/transport components in lanthanide biology. | MNNG increased mutation frequency by 1–2 orders of magnitude; selected isolates carried 1–57 point mutations. | Groom et al., 2019 | https://doi.org/10.1128/JB.00120-19 | (groom2019amutagenicscreen pages 2-5) |
| Extracellular/periplasmic Ln accumulation | RH AL1 data support compartmentalized lanthanide handling in methylotrophs, with extracellular accumulation at OMVs and intracellular storage in the periplasm, consistent with a role for TBDRs at the cell surface in selective metal acquisition. | Extracellular crystals up to 200 nm; 66.2% of cell clusters had crystalline structures contacting OMVs; clustering around crystals averaged 28.61% ± 1.75%. | Wegner et al., 2021 | https://doi.org/10.1128/AEM.03144-20 | (wegner2021extracellularandintracellular pages 2-5, wegner2021extracellularandintracellular pages 1-2) |
| TBDT structure / energy coupling | TonB-dependent transporters are outer-membrane β-barrel proteins occluded by a plug domain; TonB binds the conserved TonB box, and proton-motive-force energy is transmitted from the ExbB–ExbD complex to open the transporter for substrate passage into the periplasm. | ExbB5–ExbD2 stoichiometry; FhuA model is a 22-strand β-barrel; ferrichrome Kd ~0.1 μM; TonB box mutations can abolish uptake. | Braun, 2024 | https://doi.org/10.1111/mmi.15332 | (braun2024substrateuptakeby pages 14-15, braun2024substrateuptakeby pages 1-2, braun2024substrateuptakeby pages 2-4, braun2024substrateuptakeby pages 4-6) |
| Functional annotation relevance to C5B1I1-like proteins | For an uncharacterized TonB-dependent siderophore receptor such as UniProt C5B1I1, the strongest evidence-based annotation is outer-membrane, TonB/ExbB/ExbD-coupled uptake of a scarce metal-chelate or siderophore-like substrate into the periplasm; exact ligand specificity remains unresolved without locus-specific experiments. | Family-level features include plug domain, TonB box, and β-barrel architecture; substrate identity unresolved for the specific accession. | Braun, 2024; Roszczenko-Jasińska et al., 2020; Zytnick et al., 2022 | https://doi.org/10.1111/mmi.15332 ; https://doi.org/10.1038/s41598-020-69401-4 ; https://doi.org/10.1101/2022.01.19.476857 | (roszczenkojasinska2020geneproductsand pages 7-10, zytnick2022discoveryandcharacterization pages 1-3, braun2024substrateuptakeby pages 1-2) |
Table: This table compiles the most relevant evidence for annotating TonB-dependent receptors in methylotrophs, combining AM1-specific lanthanide uptake studies with recent mechanistic review data on TBDT structure and energy coupling. It is useful for distinguishing well-supported family-level functions from unresolved substrate-specific claims for the target protein.
Recommended primary annotation (high confidence): TonB-dependent outer-membrane β-barrel receptor/transporter with plug domain; energized by TonB–ExbB–ExbD; mediates active uptake of an extracellular scarce nutrient into the periplasm (braun2024substrateuptakeby pages 1-2, braun2024substrateuptakeby pages 4-6).
Recommended substrate annotation (moderate/low confidence): “siderophore/metal-chelate uptake receptor; specific ligand unknown.” If downstream genomic context supports iron uptake or a defined siderophore system, that should be confirmed experimentally before naming the ligand.
Localization: outer membrane (TBDT); functionally interfaces with periplasm (ligand delivery) and requires inner-membrane TonB/ExbB/ExbD machinery (braun2024substrateuptakeby pages 1-2).
Caveat on gene symbol mapping: the label mluA is not corroborated in the retrieved AM1 primary literature for this accession; do not equate it to AM1 LutH or other characterized receptors without locus-specific evidence (roszczenkojasinska2020geneproductsand pages 6-7, roszczenkojasinska2020geneproductsand pages 7-10).
References
(braun2024substrateuptakeby pages 1-2): Volkmar Braun. Substrate uptake by tonb‐dependent outer membrane transporters. Molecular Microbiology, 122:929-947, Dec 2024. URL: https://doi.org/10.1111/mmi.15332, doi:10.1111/mmi.15332. This article has 19 citations and is from a domain leading peer-reviewed journal.
(braun2024substrateuptakeby pages 2-4): Volkmar Braun. Substrate uptake by tonb‐dependent outer membrane transporters. Molecular Microbiology, 122:929-947, Dec 2024. URL: https://doi.org/10.1111/mmi.15332, doi:10.1111/mmi.15332. This article has 19 citations and is from a domain leading peer-reviewed journal.
(braun2024substrateuptakeby pages 4-6): Volkmar Braun. Substrate uptake by tonb‐dependent outer membrane transporters. Molecular Microbiology, 122:929-947, Dec 2024. URL: https://doi.org/10.1111/mmi.15332, doi:10.1111/mmi.15332. This article has 19 citations and is from a domain leading peer-reviewed journal.
(roszczenkojasinska2020geneproductsand pages 6-7): Paula Roszczenko-Jasińska, Huong N. Vu, Gabriel A. Subuyuj, Ralph Valentine Crisostomo, James Cai, Nicholas F. Lien, Erik J. Clippard, Elena M. Ayala, Richard T. Ngo, Fauna Yarza, Justin P. Wingett, Charumathi Raghuraman, Caitlin A. Hoeber, Norma C. Martinez-Gomez, and Elizabeth Skovran. Gene products and processes contributing to lanthanide homeostasis and methanol metabolism in methylorubrum extorquens am1. Scientific Reports, Jul 2020. URL: https://doi.org/10.1038/s41598-020-69401-4, doi:10.1038/s41598-020-69401-4. This article has 98 citations and is from a peer-reviewed journal.
(roszczenkojasinska2020geneproductsand pages 7-10): Paula Roszczenko-Jasińska, Huong N. Vu, Gabriel A. Subuyuj, Ralph Valentine Crisostomo, James Cai, Nicholas F. Lien, Erik J. Clippard, Elena M. Ayala, Richard T. Ngo, Fauna Yarza, Justin P. Wingett, Charumathi Raghuraman, Caitlin A. Hoeber, Norma C. Martinez-Gomez, and Elizabeth Skovran. Gene products and processes contributing to lanthanide homeostasis and methanol metabolism in methylorubrum extorquens am1. Scientific Reports, Jul 2020. URL: https://doi.org/10.1038/s41598-020-69401-4, doi:10.1038/s41598-020-69401-4. This article has 98 citations and is from a peer-reviewed journal.
(braun2024substrateuptakeby pages 14-15): Volkmar Braun. Substrate uptake by tonb‐dependent outer membrane transporters. Molecular Microbiology, 122:929-947, Dec 2024. URL: https://doi.org/10.1111/mmi.15332, doi:10.1111/mmi.15332. This article has 19 citations and is from a domain leading peer-reviewed journal.
(celia2026advancesinunderstanding pages 8-9): Herve Celia, Susan K. Buchanan, and Istvan Botos. Advances in understanding ton and tol system motor proteins. Biochemical Society Transactions, 54:107-119, Jan 2026. URL: https://doi.org/10.1042/bst20253128, doi:10.1042/bst20253128. This article has 0 citations and is from a peer-reviewed journal.
(roszczenkojasinska2020geneproductsand pages 10-11): Paula Roszczenko-Jasińska, Huong N. Vu, Gabriel A. Subuyuj, Ralph Valentine Crisostomo, James Cai, Nicholas F. Lien, Erik J. Clippard, Elena M. Ayala, Richard T. Ngo, Fauna Yarza, Justin P. Wingett, Charumathi Raghuraman, Caitlin A. Hoeber, Norma C. Martinez-Gomez, and Elizabeth Skovran. Gene products and processes contributing to lanthanide homeostasis and methanol metabolism in methylorubrum extorquens am1. Scientific Reports, Jul 2020. URL: https://doi.org/10.1038/s41598-020-69401-4, doi:10.1038/s41598-020-69401-4. This article has 98 citations and is from a peer-reviewed journal.
(roszczenkojasinska2020geneproductsand pages 1-4): Paula Roszczenko-Jasińska, Huong N. Vu, Gabriel A. Subuyuj, Ralph Valentine Crisostomo, James Cai, Nicholas F. Lien, Erik J. Clippard, Elena M. Ayala, Richard T. Ngo, Fauna Yarza, Justin P. Wingett, Charumathi Raghuraman, Caitlin A. Hoeber, Norma C. Martinez-Gomez, and Elizabeth Skovran. Gene products and processes contributing to lanthanide homeostasis and methanol metabolism in methylorubrum extorquens am1. Scientific Reports, Jul 2020. URL: https://doi.org/10.1038/s41598-020-69401-4, doi:10.1038/s41598-020-69401-4. This article has 98 citations and is from a peer-reviewed journal.
(daumann2022aperspectiveon pages 5-8): Lena J. Daumann, Arjan Pol, Huub J.M. Op den Camp, and N. Cecilia Martinez-Gomez. A perspective on the role of lanthanides in biology: discovery, open questions and possible applications. Advances in microbial physiology, 81:1-24, Jan 2022. URL: https://doi.org/10.1016/bs.ampbs.2022.06.001, doi:10.1016/bs.ampbs.2022.06.001. This article has 21 citations and is from a peer-reviewed journal.
(roszczenkojasinska2019lanthanidetransportstorage pages 1-5): Paula Roszczenko-Jasińska, Huong N. Vu, Gabriel A. Subuyuj, Ralph Valentine Crisostomo, Elena M. Ayala, James Cai, Nicholas F. Lien, Erik J. Clippard, Richard T. Ngo, Fauna Yarza, Justin P. Wingett, Charumathi Raghuraman, Caitlin A. Hoeber, Norma C. Martinez-Gomez, and Elizabeth Skovran. Lanthanide transport, storage, and beyond: genes and processes contributing to xoxf function in methylorubrum extorquens am1. bioRxiv, May 2019. URL: https://doi.org/10.1101/647677, doi:10.1101/647677. This article has 11 citations.
(shiina2023identificationofa pages 2-5): Wataru Shiina, Hidehiro Ito, and Toshiaki Kamachi. Identification of a tonb-dependent receptor involved in lanthanide switch by the characterization of laboratory-adapted methylosinus trichosporium ob3b. Applied and Environmental Microbiology, Jan 2023. URL: https://doi.org/10.1128/aem.01413-22, doi:10.1128/aem.01413-22. This article has 6 citations and is from a peer-reviewed journal.
(wegner2021extracellularandintracellular pages 1-2): Carl-Eric Wegner, Martin Westermann, Frank Steiniger, Linda Gorniak, Rohit Budhraja, Lorenz Adrian, and Kirsten Küsel. Extracellular and intracellular lanthanide accumulation in the methylotrophic beijerinckiaceae bacterium rh al1. Jun 2021. URL: https://doi.org/10.1128/aem.03144-20, doi:10.1128/aem.03144-20. This article has 32 citations and is from a peer-reviewed journal.
(daumann2022aperspectiveon pages 15-19): Lena J. Daumann, Arjan Pol, Huub J.M. Op den Camp, and N. Cecilia Martinez-Gomez. A perspective on the role of lanthanides in biology: discovery, open questions and possible applications. Advances in microbial physiology, 81:1-24, Jan 2022. URL: https://doi.org/10.1016/bs.ampbs.2022.06.001, doi:10.1016/bs.ampbs.2022.06.001. This article has 21 citations and is from a peer-reviewed journal.
(daumann2022aperspectiveon pages 11-15): Lena J. Daumann, Arjan Pol, Huub J.M. Op den Camp, and N. Cecilia Martinez-Gomez. A perspective on the role of lanthanides in biology: discovery, open questions and possible applications. Advances in microbial physiology, 81:1-24, Jan 2022. URL: https://doi.org/10.1016/bs.ampbs.2022.06.001, doi:10.1016/bs.ampbs.2022.06.001. This article has 21 citations and is from a peer-reviewed journal.
(zytnick2022discoveryandcharacterization pages 1-3): Alexa M. Zytnick, Sophie M. Gutenthaler-Tietze, Allegra T. Aron, Zachary L. Reitz, Manh Tri Phi, Nathan M. Good, Daniel Petras, Lena J. Daumann, and N. Cecilia Martinez-Gomez. Discovery and characterization of the first known biological lanthanide chelator. bioRxiv, Jan 2022. URL: https://doi.org/10.1101/2022.01.19.476857, doi:10.1101/2022.01.19.476857. This article has 20 citations.
(juma2022siderophoreforlanthanide pages 9-10): Patrick Otieno Juma, Yoshiko Fujitani, Ola Alessa, Tokitaka Oyama, Hiroya Yurimoto, Yasuyoshi Sakai, and Akio Tani. Siderophore for lanthanide and iron uptake for methylotrophy and plant growth promotion in methylobacterium aquaticum strain 22a. Frontiers in Microbiology, Jul 2022. URL: https://doi.org/10.3389/fmicb.2022.921635, doi:10.3389/fmicb.2022.921635. This article has 55 citations and is from a peer-reviewed journal.
(roszczenkojasinska2020geneproductsand media 5258917a): Paula Roszczenko-Jasińska, Huong N. Vu, Gabriel A. Subuyuj, Ralph Valentine Crisostomo, James Cai, Nicholas F. Lien, Erik J. Clippard, Elena M. Ayala, Richard T. Ngo, Fauna Yarza, Justin P. Wingett, Charumathi Raghuraman, Caitlin A. Hoeber, Norma C. Martinez-Gomez, and Elizabeth Skovran. Gene products and processes contributing to lanthanide homeostasis and methanol metabolism in methylorubrum extorquens am1. Scientific Reports, Jul 2020. URL: https://doi.org/10.1038/s41598-020-69401-4, doi:10.1038/s41598-020-69401-4. This article has 98 citations and is from a peer-reviewed journal.
(groom2019amutagenicscreen pages 2-5): Joseph D. Groom, Stephanie M. Ford, Mitchell W. Pesesky, and Mary E. Lidstrom. A mutagenic screen identifies a tonb-dependent receptor required for the lanthanide metal switch in the type i methanotroph “methylotuvimicrobium buryatense” 5gb1c. Journal of Bacteriology, Aug 2019. URL: https://doi.org/10.1128/jb.00120-19, doi:10.1128/jb.00120-19. This article has 62 citations and is from a peer-reviewed journal.
(wegner2021extracellularandintracellular pages 2-5): Carl-Eric Wegner, Martin Westermann, Frank Steiniger, Linda Gorniak, Rohit Budhraja, Lorenz Adrian, and Kirsten Küsel. Extracellular and intracellular lanthanide accumulation in the methylotrophic beijerinckiaceae bacterium rh al1. Jun 2021. URL: https://doi.org/10.1128/aem.03144-20, doi:10.1128/aem.03144-20. This article has 32 citations and is from a peer-reviewed journal.