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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 target in scope is xoxJ from Methylorubrum extorquens strain AM1 (formerly Methylobacterium extorquens AM1), corresponding to locus MexAM1_META1p1742 and annotated as a periplasmic binding protein in the xox1 operon (xoxF1GJ), adjacent to xoxF1 (Ln-dependent methanol dehydrogenase) and xoxG (partner c-type cytochrome). This matches the UniProt description for C5B122 as a solute-binding/periplasmic-binding-protein family protein with relevant domains and a role linked to quinoprotein dehydrogenase systems. (roszczenkojasinska2020geneproductsand pages 5-6, roszczenkojasinska2020geneproductsand pages 4-5, featherston2019biochemicalandstructural pages 6-7)
M. extorquens AM1 contains both (i) a Ca2+-dependent methanol dehydrogenase system (MxaFI) and (ii) lanthanide (Ln3+)-dependent PQQ alcohol dehydrogenases, notably XoxF-type methanol dehydrogenases (XoxF1 and XoxF2). When lanthanides are available, expression shifts toward the xox1 operon (xoxF1GJ) and away from the mxa operon—this regulatory remodeling is widely referred to as the lanthanide switch / rare-earth switch. (roszczenkojasinska2020geneproductsand pages 4-5)
In methylotrophs, PQQ-ADHs are periplasmic enzymes that pass electrons to a partner c-type cytochrome (e.g., XoxG), supporting respiratory electron transport. In addition to the electron-accepting cytochrome (XoxG), xoxF or exaF clusters often encode homologs of mxaJ, including xoxJ, described as periplasmic binding proteins suggested to aid activation of PQQ-ADHs. (roszczenkojasinska2020geneproductsand pages 4-5)
XoxJ is best supported as a periplasmic accessory/activation factor (a periplasmic binding protein-like fold), not a catalytic enzyme. In AM1, xoxJ is explicitly annotated as a “Periplasmic binding protein” and is genetically coupled to lanthanide-dependent methanol oxidation via its colocalization with xoxF1 and xoxG (xoxF1GJ). (roszczenkojasinska2020geneproductsand pages 5-6, roszczenkojasinska2020geneproductsand pages 4-5)
A key mechanistic advance is the X-ray crystal structure of XoxJ from M. extorquens AM1. XoxJ is a periplasmic binding protein (PBP)-fold protein whose structure reveals a large hydrophobic cavity/cleft (reported central cavity ~1750 Å3) and disordered loops, consistent with binding a large hydrophobic partner rather than a small metabolite substrate. (featherston2019biochemicalandstructural pages 18-25)
Featherston et al. propose a chaperone-like activation model: XoxJ may bind a hydrophobic region of partially folded apo-XoxF to facilitate cofactor insertion and/or maturation of XoxF into the active holoenzyme, analogous to historic proposals for the Ca-MDH accessory protein MxaJ. Importantly, they considered a PQQ-chaperone role but report that their biochemical tests did not support that specific hypothesis, leaving “activation” as an assembly/maturation function supported primarily by structure-informed inference. (featherston2019biochemicalandstructural pages 10-12, featherston2019biochemicalandstructural pages 6-7)
Structural resources: PDB entries reported for this system include XoxJ: 6ONP and XoxG: 6ONQ. (featherston2019biochemicalandstructural pages 1-3)
Evidence in the retrieved full text supports that XoxJ is functionally linked to the XoxF/XoxG module (operon structure; mutant phenotypes), and the leading mechanistic hypothesis involves interaction with apo-XoxF during activation. However, direct binding measurements (e.g., XoxJ–XoxF affinity, direct PQQ binding, direct Ln binding) are not demonstrated in the excerpts retrieved here; thus, claims about a specific ligand (PQQ vs protein segment) remain model-based rather than experimentally proven in these texts. (featherston2019biochemicalandstructural pages 10-12, featherston2019biochemicalandstructural pages 6-7, featherston2019biochemicalandstructural pages 18-25)
Roszczenko-Jasińska et al. (2020) identified xoxJ (MexAM1_META1p1742) multiple times in a transposon screen designed to find genes required for XoxF-dependent methanol oxidation. (roszczenkojasinska2020geneproductsand pages 5-6)
Critically, ΔxoxJ produces a strong phenotype during growth on methanol:
- In methanol + La3+ medium, loss of xoxJ is reported as equivalent to loss of both xoxF1 and xoxF2, supporting that XoxJ is essential for XoxF-dependent methanol oxidation. (roszczenkojasinska2020geneproductsand pages 5-6)
- Quantitatively, Table 3 shows:
- Wild type: 0.16 ± 0.01 h−1 (MeOH + La3+)
- ΔxoxJ: 0.04 ± 0.01 h−1 (MeOH + La3+)
- ΔxoxJ also has a phenotype without La3+: 21 h lag, growth rate 0.13 h−1 on MeOH (vs wild type 0.14 ± 0.01 h−1), indicating an effect even in Ln-absent conditions. (roszczenkojasinska2020geneproductsand pages 6-7)
These quantitative phenotypes are also captured in the extracted visual evidence (Table 3 / Figure 3). (roszczenkojasinska2020geneproductsand media 78813729, roszczenkojasinska2020geneproductsand media 00cde554)
In AM1, reporter-fusion experiments showed that the growth phenotypes of xoxG and xoxJ mutants in the absence of La3+ were not due to impaired expression from the mxa promoter. This argues against a model where XoxJ only affects methanol growth indirectly through Ln-switch regulation, and supports a more direct/auxiliary role in periplasmic methanol oxidation physiology. (roszczenkojasinska2020geneproductsand pages 6-7, roszczenkojasinska2020geneproductsand pages 5-6)
In M. extorquens PA1, a ΔxoxGJ strain shows a strong growth defect in the presence of La3+ while growing normally without La3+, reinforcing that the Xox accessory module (including XoxJ) is specifically critical to the REE-dependent methanol growth state. (ochsner2019useofrare‐earth pages 9-10)
Multiple lines of evidence place XoxJ in the periplasm:
- AM1 annotation explicitly labels xoxJ as a periplasmic binding protein. (roszczenkojasinska2020geneproductsand pages 5-6)
- Structural/biochemical work purified XoxJ from the periplasm in an expression system and solved the structure consistent with a periplasmic binding protein fold. (featherston2019biochemicalandstructural pages 6-7)
The xoxF1GJ operon encodes a periplasmic methanol oxidation system: XoxF (PQQ-ADH) plus its electron acceptor XoxG (c-type cytochrome) and accessory factor XoxJ. In this system, XoxG is the physiological electron acceptor for XoxF. (roszczenkojasinska2020geneproductsand pages 4-5, featherston2019biochemicalandstructural pages 1-3)
A quantitative biochemical insight relevant to module function (though not specific to XoxJ catalysis) is that when XoxF is assayed with its physiological acceptor XoxG, Vmax is reported as broadly Ln-independent (La/Ce/Nd), but the apparent Km for XoxG increases across the Ln series from La to Nd, suggesting tuning/compatibility effects in the electron transfer partner interaction. (featherston2019biochemicalandstructural pages 9-10, featherston2019biochemicalandstructural pages 3-4)
Direct 2023–2024 experimental papers specifically dissecting XoxJ in AM1 were not retrieved in this run; however, multiple high-quality 2023–2024 studies substantially advance the system-level understanding of lanthanide-dependent methylotrophy and its applications, which frames current interpretation of xoxJ.
A 2024 metagenomic study of weathered granites and soils reconstructed 136 genomes (11 bacterial phyla) and found lanthanide-dependent PQQ-ADH systems to be common. In quantitative terms, dereplication of PQQ-ADH sequences yielded 411 distinct sequences, all XoxF types; XoxF3 dominated (340 sequences) with XoxF5 next (63); notably, no mxaF was detected in these datasets. This supports the view that xox-associated systems (including accessory genes like xoxG and sometimes xoxJ) are major players in real environments where lanthanides are often mineral-bound and poorly soluble. (voutsinos2024weatheredgranitesand pages 2-4)
In a lanthanide-accumulating methylotroph (Beijerinckiaceae bacterium RH AL1), RNA-seq showed that varying La concentration (50 nM vs 1 µM) or changing Ln identity (La vs Nd vs Ln cocktail) can cause extremely broad transcriptional remodeling: up to 41% of encoded genes were differentially expressed. This supports a modern view that Ln are not merely enzyme cofactors but also major physiological regulators, and it helps explain why accessory proteins and uptake/trafficking networks are under strong selection and regulation in Ln-dependent methylotrophs. (gorniak2023differentlanthanideelements pages 1-2)
Two 2024 directions illustrate real-world implementations arising from Ln biology:
- Protein-based lanthanide separation: a 2024 PNAS study reports structural characterization of a bacterial lanthanide uptake-associated chaperone (LanD) and positions engineered protein interfaces as a strategy for separating adjacent light lanthanides; multiple LanD structures were deposited to the PDB (June 13, 2024). While not about xoxJ directly, this is a concrete translation pathway from Ln-dependent methylotroph biology into separations technology. (larrinaga2024modulatingmetalcentereddimerization pages 8-8)
- Artificial metalloenzyme platforms: a 2024 PNAS study describes a biomimetic La3+-PQQ artificial metalloprotein as a platform for mechanistic interrogation of rare-earth PQQ-ADHs; the work explicitly frames XoxJ and XoxG as accessory proteins in natural Xox systems, motivating simplified engineered surrogates. (thompson2024structuredrivendevelopmentof; retrieved but not fully evidenced in excerpts here)
Across genetic and structural studies, the prevailing expert interpretation is that XoxJ is an accessory activation factor required for the functional expression of lanthanide-dependent methanol oxidation, with an as-yet incompletely defined molecular mechanism. The strongest direct evidence is genetic necessity (phenocopy of xoxF1/xoxF2 loss under Ln conditions) combined with structure-informed hypotheses about apo-enzyme maturation. (roszczenkojasinska2020geneproductsand pages 5-6, featherston2019biochemicalandstructural pages 10-12)
Recommended annotation (evidence-weighted):
- Protein type: Periplasmic binding protein-like accessory factor (PBP fold). (roszczenkojasinska2020geneproductsand pages 5-6, featherston2019biochemicalandstructural pages 6-7)
- Primary biological role: Required for lanthanide-dependent methanol growth and XoxF-dependent methanol oxidation, likely by enabling activation/maturation of XoxF in the periplasm (assembly/cofactor insertion chaperone-like function). (roszczenkojasinska2020geneproductsand pages 5-6, featherston2019biochemicalandstructural pages 10-12)
- Localization: Periplasm. (roszczenkojasinska2020geneproductsand pages 5-6, featherston2019biochemicalandstructural pages 6-7)
- Pathway context: xoxF1GJ module within lanthanide-dependent methylotrophy; interfaces with electron transfer via XoxG. (roszczenkojasinska2020geneproductsand pages 4-5, featherston2019biochemicalandstructural pages 1-3)
| Claim/annotation | Evidence type (genetic/biochemical/structural) | Key findings | Source (authors, year, journal) | DOI/URL | Context ID(s) |
|---|---|---|---|---|---|
| xoxJ (MexAM1_META1p1742; UniProt C5B122) in Methylorubrum extorquens AM1 is annotated as a periplasmic binding protein | Genetic/genome annotation | Identified in transposon screen; Table 1 annotates xoxJ as “Periplasmic binding protein.” XoxJ is described as a homolog of MxaJ, part of xox/exa systems associated with periplasmic PQQ-ADHs | Roszczenko-Jasińska et al., 2020, Scientific Reports | https://doi.org/10.1038/s41598-020-69401-4 | (roszczenkojasinska2020geneproductsand pages 5-6, roszczenkojasinska2020geneproductsand pages 4-5) |
| xoxJ is genomically linked to the lanthanide-dependent MDH system | Genetic/genomic context | xoxJ lies adjacent to xoxG and xoxF1 in the xox1 operon (xoxF1GJ), supporting functional coupling to Ln-dependent methanol oxidation and the Ln-switch | Roszczenko-Jasińska et al., 2020, Scientific Reports | https://doi.org/10.1038/s41598-020-69401-4 | (roszczenkojasinska2020geneproductsand pages 4-5) |
| XoxJ is a periplasmic protein with a canonical periplasmic binding protein fold | Structural/biochemical | XoxJ was expressed in E. coli, purified from the periplasm, and crystallized at 2.27 Å; structure shows the characteristic two-domain PBP fold with a putative substrate-binding cavity | Featherston et al., 2019, ChemBioChem | https://doi.org/10.1002/cbic.201900184 | (featherston2019biochemicalandstructural pages 6-7) |
| XoxJ has distinctive structural features consistent with an accessory/chaperone role rather than transport | Structural | Crystal structure reveals a large hydrophobic cleft/cavity; central cavity reported as ~1750 ų, surrounded by disordered loops. PDB depositions: XoxJ 6ONP; XoxG 6ONQ | Featherston et al., 2019, ChemBioChem | https://doi.org/10.1002/cbic.201900184 | (featherston2019biochemicalandstructural pages 18-25, featherston2019biochemicalandstructural pages 1-3) |
| XoxJ is not supported as a PQQ chaperone by available biochemical tests | Biochemical/structural inference | Authors considered XoxJ as a possible PQQ chaperone, but biochemical data did not support that specific role | Featherston et al., 2019, ChemBioChem | https://doi.org/10.1002/cbic.201900184 | (featherston2019biochemicalandstructural pages 10-12, featherston2019biochemicalandstructural pages 9-10) |
| Current best mechanistic model is that XoxJ helps activate apo-XoxF during assembly/cofactor insertion | Structural/mechanistic inference | Large hydrophobic cleft and similarity to MxaJ suggest XoxJ binds a hydrophobic region of partially folded apo-XoxF, helping cofactor insertion/activation; holo-XoxF is dimeric whereas PQQ loss causes monomerization, supporting a role in maturation rather than catalysis | Featherston et al., 2019, ChemBioChem; Pastawan et al., 2020, Reviews in Agricultural Science | https://doi.org/10.1002/cbic.201900184; https://doi.org/10.7831/ras.8.0_186 | (featherston2019biochemicalandstructural pages 10-12, featherston2019biochemicalandstructural pages 6-7) |
| xoxJ is required for normal lanthanide-dependent methanol growth in AM1 | Genetic/physiological | In methanol + La³⁺ medium, loss of xoxJ was “equivalent to loss of both xoxF1 and xoxF2,” supporting that XoxJ is essential for XoxF-dependent methanol oxidation | Roszczenko-Jasińska et al., 2020, Scientific Reports | https://doi.org/10.1038/s41598-020-69401-4 | (roszczenkojasinska2020geneproductsand pages 5-6) |
| Quantitative phenotype of ΔxoxJ in AM1 without lanthanum | Genetic/physiological | On methanol without La³⁺, ΔxoxJ showed a 21 h lag and growth rate 0.13 h⁻¹; wild type grew at 0.14 ± 0.01 h⁻¹. This indicates a phenotype even when La³⁺ is absent | Roszczenko-Jasińska et al., 2020, Scientific Reports | https://doi.org/10.1038/s41598-020-69401-4 | (roszczenkojasinska2020geneproductsand pages 6-7) |
| Quantitative phenotype of ΔxoxJ in AM1 with lanthanum | Genetic/physiological | On methanol + La³⁺, ΔxoxJ grew at 0.04 ± 0.01 h⁻¹ versus wild type 0.16 ± 0.01 h⁻¹, matching the severe defect of the xoxF1 xoxF2 mutant in La³⁺ medium | Roszczenko-Jasińska et al., 2020, Scientific Reports | https://doi.org/10.1038/s41598-020-69401-4 | (roszczenkojasinska2020geneproductsand pages 6-7, roszczenkojasinska2020geneproductsand pages 5-6, roszczenkojasinska2020geneproductsand media 78813729, roszczenkojasinska2020geneproductsand media 00cde554) |
| xoxJ mutant phenotypes are not explained simply by failed mxa induction | Genetic/regulatory | Reporter fusions showed the ΔxoxJ growth defect in the absence of La³⁺ was not due to impaired mxa promoter expression, implying XoxJ may have a broader/direct role in methanol metabolism beyond Ln-switch regulation | Roszczenko-Jasińska et al., 2020, Scientific Reports | https://doi.org/10.1038/s41598-020-69401-4 | (roszczenkojasinska2020geneproductsand pages 6-7, roszczenkojasinska2020geneproductsand pages 5-6) |
| Independent preprint evidence also linked XoxJ to XoxF activity | Genetic/inference | Deletion of xoxJ reportedly mirrored the xoxF1 xoxF2 double mutant; authors interpreted this as consistent with XoxJ interacting with and possibly activating XoxF | Roszczenko-Jasińska et al., 2019, bioRxiv | https://doi.org/10.1101/647677 | (roszczenkojasinska2019lanthanidetransportstorage pages 15-18) |
| Related strain PA1 shows a severe La-dependent phenotype when xoxGJ are deleted | Genetic/physiological | In M. extorquens PA1, a ΔxoxGJ strain grew normally without La³⁺ but had a strong growth defect in the presence of La³⁺, reinforcing the requirement of XoxG/J for REE-dependent methanol metabolism | Ochsner et al., 2019, Molecular Microbiology | https://doi.org/10.1111/mmi.14208 | (ochsner2019useofrare‐earth pages 9-10) |
| XoxG is the physiological electron acceptor paired with XoxF; this informs the XoxJ/XoxFGJ system | Biochemical/structural | XoxG is a c-type cytochrome serving as XoxF’s physiological electron acceptor; XoxF activity with La³⁺, Ce³⁺, and Nd³⁺ is similar in Vmax when assayed with XoxG, indicating the accessory system supports multiple light Ln cofactors | Featherston et al., 2019, ChemBioChem | https://doi.org/10.1002/cbic.201900184 | (featherston2019biochemicalandstructural pages 9-10, featherston2019biochemicalandstructural pages 1-3) |
| XoxG has a low reduction potential tuned for the XoxF system | Biochemical/structural | XoxG has an unusually low midpoint reduction potential of about +172 mV; structural analysis attributes this to a distinctive, relatively solvent-exposed heme environment | Featherston et al., 2019, ChemBioChem | https://doi.org/10.1002/cbic.201900184 | (featherston2019biochemicalandstructural pages 9-10, featherston2019biochemicalandstructural pages 1-3) |
| Ln-dependent changes in apparent Km for XoxG suggest co-adaptation within the XoxFGJ system | Biochemical/kinetic | With XoxG as electron acceptor, XoxF Vmax values were not significantly different across La/Ce/Nd, but apparent Km for XoxG increased markedly from La to Nd; a predicted ~10 μM Km was noted for Sm-XoxF, supporting tuning of the XoxF–XoxG pair to lighter lanthanides | Featherston et al., 2019, ChemBioChem | https://doi.org/10.1002/cbic.201900184 | (featherston2019biochemicalandstructural pages 9-10, featherston2019biochemicalandstructural pages 3-4) |
Table: This table summarizes the strongest available evidence for functional annotation of xoxJ (UniProt C5B122) in Methylorubrum extorquens AM1, integrating genetic, biochemical, and structural data. It highlights what is directly supported experimentally versus what remains mechanistic inference, which is useful for cautious gene/protein annotation.
References
(roszczenkojasinska2020geneproductsand pages 5-6): 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 92 citations and is from a peer-reviewed journal.
(roszczenkojasinska2020geneproductsand pages 4-5): 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 92 citations and is from a peer-reviewed journal.
(featherston2019biochemicalandstructural pages 6-7): Emily R. Featherston, Hannah R. Rose, Molly J. McBride, Ellison M. Taylor, Amie K. Boal, and Joseph A. Cotruvo. Biochemical and structural characterization of xoxg and xoxj and their roles in lanthanide‐dependent methanol dehydrogenase activity. ChemBioChem, 20:2360-2372, Sep 2019. URL: https://doi.org/10.1002/cbic.201900184, doi:10.1002/cbic.201900184. This article has 55 citations and is from a peer-reviewed journal.
(featherston2019biochemicalandstructural pages 18-25): Emily R. Featherston, Hannah R. Rose, Molly J. McBride, Ellison M. Taylor, Amie K. Boal, and Joseph A. Cotruvo. Biochemical and structural characterization of xoxg and xoxj and their roles in lanthanide‐dependent methanol dehydrogenase activity. ChemBioChem, 20:2360-2372, Sep 2019. URL: https://doi.org/10.1002/cbic.201900184, doi:10.1002/cbic.201900184. This article has 55 citations and is from a peer-reviewed journal.
(featherston2019biochemicalandstructural pages 10-12): Emily R. Featherston, Hannah R. Rose, Molly J. McBride, Ellison M. Taylor, Amie K. Boal, and Joseph A. Cotruvo. Biochemical and structural characterization of xoxg and xoxj and their roles in lanthanide‐dependent methanol dehydrogenase activity. ChemBioChem, 20:2360-2372, Sep 2019. URL: https://doi.org/10.1002/cbic.201900184, doi:10.1002/cbic.201900184. This article has 55 citations and is from a peer-reviewed journal.
(featherston2019biochemicalandstructural pages 1-3): Emily R. Featherston, Hannah R. Rose, Molly J. McBride, Ellison M. Taylor, Amie K. Boal, and Joseph A. Cotruvo. Biochemical and structural characterization of xoxg and xoxj and their roles in lanthanide‐dependent methanol dehydrogenase activity. ChemBioChem, 20:2360-2372, Sep 2019. URL: https://doi.org/10.1002/cbic.201900184, doi:10.1002/cbic.201900184. This article has 55 citations and is from a 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 92 citations and is from a peer-reviewed journal.
(roszczenkojasinska2020geneproductsand media 78813729): 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 92 citations and is from a peer-reviewed journal.
(roszczenkojasinska2020geneproductsand media 00cde554): 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 92 citations and is from a peer-reviewed journal.
(ochsner2019useofrare‐earth pages 9-10): Andrea M. Ochsner, Lucas Hemmerle, Thomas Vonderach, Ralph Nüssli, Miriam Bortfeld‐Miller, Bodo Hattendorf, and Julia A. Vorholt. Use of rare‐earth elements in the phyllosphere colonizer methylobacterium extorquens pa1. Molecular Microbiology, 111:1152-1166, Feb 2019. URL: https://doi.org/10.1111/mmi.14208, doi:10.1111/mmi.14208. This article has 145 citations and is from a domain leading peer-reviewed journal.
(featherston2019biochemicalandstructural pages 9-10): Emily R. Featherston, Hannah R. Rose, Molly J. McBride, Ellison M. Taylor, Amie K. Boal, and Joseph A. Cotruvo. Biochemical and structural characterization of xoxg and xoxj and their roles in lanthanide‐dependent methanol dehydrogenase activity. ChemBioChem, 20:2360-2372, Sep 2019. URL: https://doi.org/10.1002/cbic.201900184, doi:10.1002/cbic.201900184. This article has 55 citations and is from a peer-reviewed journal.
(featherston2019biochemicalandstructural pages 3-4): Emily R. Featherston, Hannah R. Rose, Molly J. McBride, Ellison M. Taylor, Amie K. Boal, and Joseph A. Cotruvo. Biochemical and structural characterization of xoxg and xoxj and their roles in lanthanide‐dependent methanol dehydrogenase activity. ChemBioChem, 20:2360-2372, Sep 2019. URL: https://doi.org/10.1002/cbic.201900184, doi:10.1002/cbic.201900184. This article has 55 citations and is from a peer-reviewed journal.
(voutsinos2024weatheredgranitesand pages 2-4): Marcos Y. Voutsinos, Jacob A. West-Roberts, Rohan Sachdeva, John W. Moreau, and Jillian F. Banfield. Weathered granites and soils harbour microbes with lanthanide-dependent methylotrophic enzymes. BMC Biology, Feb 2024. URL: https://doi.org/10.1186/s12915-024-01841-0, doi:10.1186/s12915-024-01841-0. This article has 13 citations and is from a domain leading peer-reviewed journal.
(gorniak2023differentlanthanideelements pages 1-2): Linda Gorniak, Julia Bechwar, Martin Westermann, Frank Steiniger, and Carl-Eric Wegner. Different lanthanide elements induce strong gene expression changes in a lanthanide-accumulating methylotroph. Dec 2023. URL: https://doi.org/10.1128/spectrum.00867-23, doi:10.1128/spectrum.00867-23. This article has 17 citations and is from a domain leading peer-reviewed journal.
(larrinaga2024modulatingmetalcentereddimerization pages 8-8): Wyatt B. Larrinaga, Jonathan J. Jung, Chi-Yun Lin, Amie K. Boal, and Joseph A. Cotruvo. Modulating metal-centered dimerization of a lanthanide chaperone protein for separation of light lanthanides. Proceedings of the National Academy of Sciences of the United States of America, Oct 2024. URL: https://doi.org/10.1073/pnas.2410926121, doi:10.1073/pnas.2410926121. This article has 25 citations and is from a highest quality peer-reviewed journal.
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