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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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.
MxbM (UniProt C5B132) is a two-component transcriptional response regulator in the model facultative methylotroph Methylorubrum extorquens strain AM1 (formerly Methylobacterium extorquens AM1). Genomic context places mxbM adjacent to mxbD, consistent with a cognate sensor kinase/response regulator pair (MxbD–MxbM) in the methanol oxidation (MOX) gene cluster. Functional genetics summarized in reviews and primary work indicate MxbM is required for activation of the Ca2+-dependent methanol dehydrogenase system (mxa operon) and is uniquely required for repression of the lanthanide-dependent methanol dehydrogenase system (xox1 operon) under particular conditions, positioning MxbM as a core regulatory element of the “lanthanide switch” that toggles between methanol oxidation modules in response to rare earth elements. However, despite strong genetic evidence, direct biochemical demonstration of MxbM’s phosphorylation state dynamics and direct DNA binding at target promoters is not established in the retrieved sources, so mechanistic details remain partly inferred.
Organism and gene identity. The target gene mxbM is from Methylorubrum extorquens strain AM1 (ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1), matching the user-provided UniProt organism context. A genomic review of AM1 methylotrophy annotates mxbM (also referenced historically as moxM) as a transcriptional regulator in a methanol-oxidation gene cluster, adjacent to mxbD/moxD, annotated as a sensor kinase (two-component pair). This supports that the “mxbM” in the methylotrophy literature corresponds to the same response-regulator module described in UniProt. (chistoserdova2003methylotrophyinmethylobacterium pages 2-3)
Symbol ambiguity. Within the retrieved evidence, “mxbM” is consistently used in the AM1 methylotrophy regulatory context (MxbDM controlling methanol oxidation gene expression), and no alternate “mxbM” identity in other organisms conflicted with this target. (chistoserdova2003methylotrophyinmethylobacterium pages 2-3, skovran2019lanthanidesinmethylotrophy pages 6-8)
A bacterial two-component system classically comprises a sensor histidine kinase (HK) and a response regulator (RR). The HK senses an environmental or intracellular cue, autophosphorylates on histidine, and transfers the phosphate to a conserved aspartate in the RR receiver domain. The phosphorylated RR typically changes conformation and often acts as a DNA-binding transcription factor.
For AM1 methylotrophy regulation, MxbM functions as the RR partner of MxbD (HK) in the MxbDM TCS, and is part of a larger regulatory network controlling methanol dehydrogenase gene expression. (chistoserdova2003methylotrophyinmethylobacterium pages 2-3, skovran2019lanthanidesinmethylotrophy pages 6-8)
Many methylotrophs encode both:
- a Ca2+-dependent methanol dehydrogenase (MxaFI; “mxa operon”), and
- a lanthanide (Ln3+)-dependent methanol dehydrogenase (XoxF; “xox operon(s)”).
The lanthanide switch refers to lanthanide-dependent transcriptional control in which Ln3+ availability shifts expression between these systems: typically repressing mxa and inducing xox when lanthanides are available. In AM1, this switch is controlled by multiple regulators including MxcQE and MxbDM TCSs and an orphan response regulator MxaB, with MxbM being a critical component. (vu2016lanthanidedependentregulationof pages 6-9, skovran2019lanthanidesinmethylotrophy pages 6-8)
Across the retrieved sources, the best-supported role for MxbM is regulatory control of methanol oxidation gene expression, specifically:
- Activation of the mxa operon (MxaFI system): MxbM (along with other regulators) is required for expression of the mxa genes. (skovran2019lanthanidesinmethylotrophy pages 6-8)
- Repression of the xox1 operon: MxbM is highlighted as uniquely required for repression of the xox1 operon (relative to other regulators in the network) in AM1. (skovran2019lanthanidesinmethylotrophy pages 6-8)
A comparative review excerpt also states that MxbDM increases mxa expression while decreasing xoxF expression, consistent with a role in balancing alternative methanol dehydrogenase systems. (chu2016xoxfactsas pages 9-12)
A key “expert consensus” point emerging from an authoritative review is that AM1 methanol oxidation regulation involves at least two TCSs and an orphan RR:
- MxcQE (TCS)
- MxbDM (TCS, with MxbM as the RR)
- MxaB (orphan response regulator)
Within that network:
- MxcE, MxaB, and MxbM are reported as required for mxa expression.
- Only MxbM is required for xox1 repression.
- A cascade model has been proposed in which MxcQE activates mxbDM (i.e., MxbM is downstream of MxcQE), though this is not yet fully mechanistically resolved in the retrieved evidence. (skovran2019lanthanidesinmethylotrophy pages 6-8)
A primary experimental paper (Vu et al., 2016) examined promoter activity for mxa and xox1 using fluorescent transcriptional reporters under controlled Ca/Ln conditions, and framed the regulatory logic in terms of MxcQE and MxbDM requirements. (vu2016lanthanidedependentregulationof pages 31-40)
That work advances a mechanistic model in which XoxF itself, in its apo (metal-free) state, participates in lanthanide sensing: in the absence of lanthanides, apo-XoxF contributes to activation of mxa and repression of xox1 through the regulatory network involving MxcQE/MxbDM; in the presence of lanthanides, XoxF becomes catalytically active and no longer enforces that regulatory state, enabling the transcriptional shift. (vu2016lanthanidedependentregulationof pages 31-40)
Quantitative experimental conditions (AM1, Vu et al. 2016). Reporter assays used MP succinate-methanol media with 20 μM Ca and lanthanide concentrations ranging from 2.5 nM to 20 μM, with specific tests at 2 μM for multiple lanthanides and 20 μM Sm. The promoterless Venus background was 58 ± 5 RFU/OD600. (vu2016lanthanidedependentregulationof pages 6-9, vu2016lanthanidedependentregulationof pages 31-40)
Biochemical datapoint relevant to Ln–XoxF: the same study reports a purified XoxF dimer containing 1.24 atoms of La and lacking Ca, consistent with lanthanide occupancy of the enzyme under Ln growth conditions (context for the switch input signal). (vu2016lanthanidedependentregulationof pages 6-9)
The retrieved evidence strongly supports MxbM’s regulatory role by genetics and promoter-reporter logic, but does not provide numeric growth rates or fold-changes specifically for mxbM mutants in the snippets obtained. (vu2016lanthanidedependentregulationof pages 6-9, skovran2019lanthanidesinmethylotrophy pages 6-8, vu2016lanthanidedependentregulationof pages 31-40)
From the UniProt context supplied by the user, MxbM (C5B132) contains:
- a CheY-like response-regulator receiver domain (signal transduction receiver), and
- an OmpR/PhoB-type DNA-binding domain (winged helix-turn-helix), with WalR-like family assignment.
This architecture is consistent with a canonical transcriptional RR expected to regulate gene expression downstream of a sensor kinase such as MxbD. Genomic annotation and methylotrophy reviews align with this interpretation by describing mxbM as a transcriptional regulator/response regulator in a two-component module. (chistoserdova2003methylotrophyinmethylobacterium pages 2-3, skovran2019lanthanidesinmethylotrophy pages 6-8)
Authoritative review synthesis emphasizes an important limitation: although genetic evidence places MxbM at the center of mxa/xox1 control, direct demonstration of (i) MxbM phosphorylation state changes, and (ii) MxbM’s direct DNA binding at target promoters is not established in the retrieved evidence. Thus, the field-level understanding (from these sources) is that MxbM is a response regulator with inferred phosphorylation-dependent transcriptional control, but details of the molecular mechanism remain unresolved. (skovran2019lanthanidesinmethylotrophy pages 6-8)
No direct experimental localization of MxbM is provided in the retrieved evidence. Given its inferred role as a DNA-binding transcription factor RR, the most plausible localization is cytosolic, acting on chromosomal promoters; however, this remains a prediction rather than a demonstrated property in the retrieved sources. (skovran2019lanthanidesinmethylotrophy pages 6-8)
A 2023 study in Methylobacterium aquaticum strain 22A (a plant-associated methylotroph) reported that a methylotaxis MCP (MtpC) is regulated under MxbDM, and that MxbDM is required for MxaF expression in that organism. While not AM1-specific and not isolating MxbM biochemistry, this work provides modern evidence that the MxbDM module can connect methanol oxidation regulation to behaviors relevant to plant colonization. (tani2023metabolismlinkedmethylotaxissensors pages 1-2)
A 2024 review on pink-pigmented facultative methylotrophs (PPFMs) reiterates that methanol oxidation gene regulation involves elements including xoxF, the mxbD/mxbM sensor-regulator pair, and mxaB, situating these modules within broader agricultural and biotechnological contexts of methylotroph use. This is an applications synthesis rather than new mechanistic insight into MxbM itself. (mondal2024bioprospectsofpink pages 14-15)
Scope note: No 2023–2024 primary paper directly characterizing AM1 MxbM phosphorylation, DNA-binding sites, or regulon mapping was retrieved here.
A practical synthetic-biology implementation repurposed M. extorquens methanol-sensing regulatory modules by domain-swapping MxbD (and MxcQ) sensor regions into chimeric histidine kinases in E. coli, coupled to OmpR and an ompC promoter GFP readout. While this leverages MxbD (the sensor kinase) rather than MxbM directly, it demonstrates that the native MxbD/MxbM-associated regulatory logic can be engineered into heterologous systems for methanol detection. (selvamani2020engineeringofrecombinant pages 1-3, selvamani2020engineeringofrecombinant pages 5-8)
Quantitative sensor performance:
- Fluorescence maxima at 0.05% methanol (MxbD-derived chimera) and 0.01% methanol (MxcQ-derived chimera).
- Detection down to 0.01% methanol.
- qRT-PCR: maximum ompC expression at 2% methanol for the MxbD-derived chimera, and 0.01% for the MxcQ-derived chimera; reported correlation with methanol concentration 0.94592.
- Contextual industrial statistic in the same work: >90 methanol plants with ~100 million metric tons/year combined capacity (supporting industrial motivation for sensing/monitoring). (selvamani2020engineeringofrecombinant pages 5-8)
A 2020 study in AM1 identified gene products and processes involved in lanthanide homeostasis, including evidence that a TonB–ABC system is required for lanthanide uptake to the cytoplasm and that lanthanides can be stored as cytoplasmic inclusions (TEM/EDS). While not specific to MxbM, these findings matter for real-world deployment of lanthanide-dependent methylotrophy because Ln availability is the environmental input that drives the regulatory switch (mxa/xox). (roszczenkojasinska2020geneproductsand pages 1-4)
An authoritative review of lanthanides in methylotrophy emphasizes that for AM1 the methanol oxidation regulatory network is multi-layered (two TCSs plus an orphan RR), that MxbM is uniquely required for repression of xox1 while also contributing to mxa activation, and that key mechanistic questions (direct DNA-binding sites, phosphorylation dependence) remain unresolved despite decades of genetics. This framing provides the best available “expert consensus” perspective in the retrieved sources. (skovran2019lanthanidesinmethylotrophy pages 6-8)
| Claim/feature | Evidence summary (1–2 sentences) | Key genes/pathways | Quantitative details | Source (author-year, journal) | URL | Publication date | Citation ID |
|---|---|---|---|---|---|---|---|
| Identity: MxbM is the response regulator in the MOX cluster adjacent to mxbD | A genomic review of Methylobacterium/Methylorubrum extorquens AM1 annotates mxbM (historically moxM) as a transcriptional regulator in methylotrophy cluster 2, with neighboring mxbD/moxD annotated as a sensor kinase, consistent with a two-component sensor-regulator pair. This matches UniProt C5B132 as a two-component transcriptional regulator in AM1. (chistoserdova2003methylotrophyinmethylobacterium pages 2-3) | mxbM/moxM, mxbD/moxD; MOX cluster; methanol oxidation locus | No quantitative values reported in the excerpt | Chistoserdova et al. 2003, Journal of Bacteriology | https://doi.org/10.1128/jb.185.10.2980-2987.2003 | May 2003 | (chistoserdova2003methylotrophyinmethylobacterium pages 2-3) |
| Functional role: required for activation of the mxa operon and repression of xox1 | Review evidence summarizing experimental genetics in AM1 states that MxcE, MxaB, and MxbM are required for mxa operon expression, whereas MxbM is specifically required for repression of the xox1 operon. Independent review/excerpted summaries also describe MxbDM as increasing mxa expression while decreasing xoxF/xox1 expression. (skovran2019lanthanidesinmethylotrophy pages 6-8, chu2016xoxfactsas pages 9-12) | mxa operon (mxaFI), xox1/xoxF operon; methanol dehydrogenase expression control | No MxbM-specific fold changes reported in retrieved excerpts | Skovran et al. 2019, Current Issues in Molecular Biology; summarized in Chu & Lidstrom 2016, Journal of Bacteriology | https://doi.org/10.21775/cimb.033.101; https://doi.org/10.1128/jb.00959-15 | Jan 2019; Apr 2016 | (skovran2019lanthanidesinmethylotrophy pages 6-8, chu2016xoxfactsas pages 9-12) |
| Lanthanide-switch involvement and apo-XoxF signaling model | In AM1, lanthanide-responsive reporter studies support a model in which apo-XoxF functions as a lanthanide sensor: in the absence of lanthanides it activates mxa and represses xox1 via MxcQE/MxbDM, while lanthanide-bound XoxF no longer drives that regulatory state. The same study notes that expression from mxa and xox1 promoters is highly sensitive to La, Ce, Pr, and Nd. (vu2016lanthanidedependentregulationof pages 6-9, vu2016lanthanidedependentregulationof pages 31-40) | xoxF1, mxa, xox1, MxcQE, MxbDM; lanthanide switch | Reporter assays used 20 μM Ca and lanthanides from 2.5 nM to 20 μM; specific lanthanide tests included 2 μM lanthanides and 20 μM Sm; promoterless Venus background 58 ± 5 RFU/OD600; purified XoxF dimer contained 1.24 La atoms and no Ca. (vu2016lanthanidedependentregulationof pages 6-9, vu2016lanthanidedependentregulationof pages 31-40) | Vu et al. 2016, Journal of Bacteriology | https://doi.org/10.1128/jb.00937-15 | Apr 2016 | (vu2016lanthanidedependentregulationof pages 6-9, vu2016lanthanidedependentregulationof pages 31-40) |
| Regulatory cascade hypothesis: MxcQE → mxbDM | A regulatory cascade has been proposed in which MxcQE activates mxbDM, placing MxbM downstream of another two-component system in the methanol dehydrogenase regulatory network. This remains a model-level interpretation rather than a fully biochemically resolved pathway. (skovran2019lanthanidesinmethylotrophy pages 6-8) | MxcQE, mxbDM, mxa, xox1 | No direct quantitative cascade measurements reported in retrieved excerpts | Skovran et al. 2019, Current Issues in Molecular Biology | https://doi.org/10.21775/cimb.033.101 | Jan 2019 | (skovran2019lanthanidesinmethylotrophy pages 6-8) |
| Unresolved mechanism: phosphorylation state and direct DNA binding not shown | Reviews emphasize that although genetic evidence supports MxbM function, the phosphorylation state of the regulators and direct DNA binding have not been demonstrated. Thus, MxbM is strongly inferred to be a DNA-binding response regulator from genetics/domain architecture, but the direct molecular mechanism remains unresolved. (skovran2019lanthanidesinmethylotrophy pages 6-8) | Response-regulator signaling; transcriptional control of mxa/xox1 | No biochemical constants or phosphosite data reported in retrieved excerpts | Skovran et al. 2019, Current Issues in Molecular Biology | https://doi.org/10.21775/cimb.033.101 | Jan 2019 | (skovran2019lanthanidesinmethylotrophy pages 6-8) |
| Lanthanide-dependent growth context relevant to MxbM-regulated methanol oxidation | Review data for AM1 show that lanthanides strongly enhance methylotrophic growth conditions in which the mxa/xox switch operates, providing physiological context for the MxbM-controlled network. These data are not MxbM-specific mutant measurements but are relevant to the pathway MxbM regulates. (skovran2019lanthanidesinmethylotrophy pages 1-2) | Lanthanide-dependent methanol oxidation; mxaFI/xoxF systems | AM1 reached OD600 = 1.6 in culture tubes with 100 nM La; optimal growth rate and density were reported at 1 μM La. Environmental REE levels were noted as pico- to nanomolar, with low micromolar soluble REE in some acidic settings. (skovran2019lanthanidesinmethylotrophy pages 1-2) | Skovran et al. 2019, Current Issues in Molecular Biology | https://doi.org/10.21775/cimb.033.101 | Jan 2019 | (skovran2019lanthanidesinmethylotrophy pages 1-2) |
| Application: methanol biosensor using the mxbDM sensor domain | A synthetic biology study engineered the methanol-sensing domain of MxbD from M. extorquens into chimeric histidine kinases in E. coli, demonstrating practical reuse of the AM1 methanol-responsive regulatory system. While the engineered construct used MxbD rather than MxbM directly, it exploits the same native regulatory module historically linked to mxbDM/mxcQE/mxaB control of methanol oxidation genes. (selvamani2020engineeringofrecombinant pages 1-3, selvamani2020engineeringofrecombinant pages 5-8) | mxbDM, mxcQE, mxaB; methanol sensing; engineered two-component signaling | Maximum fluorescence at 0.05% methanol for MxbDZ and 0.01% methanol for MxcQZ; both detected as low as 0.01% methanol; maximal sensor-kinase expression at 0.5 mM IPTG; max ompC expression at 2% methanol for MxbDZ and 0.01% for MxcQZ; correlation coefficient 0.94592; allowable environmental limit cited as 200 ppm (0.02%); global methanol production context ~100 million metric tons/year across >90 plants. (selvamani2020engineeringofrecombinant pages 1-3, selvamani2020engineeringofrecombinant pages 5-8) | Selvamani et al. 2020, J. Microbiol. Biotechnol. / DOI record | https://doi.org/10.4014/mbl.1908.08009 | Mar 2020 | (selvamani2020engineeringofrecombinant pages 1-3, selvamani2020engineeringofrecombinant pages 5-8) |
| Recent 2023 link: MxbDM-regulated methylotaxis and plant colonization | In Methylobacterium aquaticum 22A, a 2023 study reports that methylotaxis sensor MtpC is regulated under MxbDM, which is also required for MxaF expression. This is not AM1-specific or MxbM-specific biochemistry, but it is recent comparative evidence that the MxbDM module can couple methanol oxidation regulation to plant-associated behavior. (tani2023metabolismlinkedmethylotaxissensors pages 1-2) | MxbDM, MxaFI, XoxF, MtpC; methylotaxis; plant colonization | Triple MCP mutant lost methylotaxis and showed slower gathering to plant tissues and reduced colonization, but the excerpt gives no numeric effect sizes for MxbDM specifically. (tani2023metabolismlinkedmethylotaxissensors pages 1-2) | Tani et al. 2023, Frontiers in Microbiology | https://doi.org/10.3389/fmicb.2023.1258452 | Oct 2023 | (tani2023metabolismlinkedmethylotaxissensors pages 1-2) |
| Lanthanide uptake/storage findings relevant to applications of the regulated pathway | Work on AM1 lanthanide homeostasis identified a TonB-ABC transport system required for lanthanide uptake, repression of the TonB receptor by excess lanthanides, and cytoplasmic lanthanide storage inclusions visualized by TEM/EDS. These findings are relevant to applications such as lanthanide biorecovery and to understanding the upstream metal availability that drives the MxbM-linked methanol oxidation switch. (roszczenkojasinska2020geneproductsand pages 1-4) | xoxF1, lanthanide transport cluster (lut context), TonB-ABC transport; lanthanide storage | Lanthanides were shown as cytoplasmic inclusions by TEM/EDS; no explicit concentration/performance numbers for biorecovery were reported in the excerpt. (roszczenkojasinska2020geneproductsand pages 1-4) | Roszczenko-Jasińska et al. 2020, Scientific Reports | https://doi.org/10.1038/s41598-020-69401-4 | Jul 2020 | (roszczenkojasinska2020geneproductsand pages 1-4) |
Table: This table summarizes the strongest available evidence for the identity, function, regulatory context, and applied relevance of MxbM/MxbDM in Methylorubrum extorquens AM1. It distinguishes experimentally supported claims from unresolved mechanistic inferences and includes quantitative details where present.
Recommended functional annotation (supported):
- Gene product: Two-component response regulator MxbM (transcriptional regulator)
- Primary biological role: Regulates expression of methanol dehydrogenase systems; required for mxa operon expression and for xox1 repression (in AM1 regulatory context). (skovran2019lanthanidesinmethylotrophy pages 6-8)
- Pathway membership: Methanol oxidation regulation / lanthanide switch network involving MxcQE, MxbDM, and MxaB, with XoxF-linked lanthanide sensing logic. (skovran2019lanthanidesinmethylotrophy pages 6-8, vu2016lanthanidedependentregulationof pages 31-40)
- Localization: Likely cytosolic DNA-binding regulator (predicted); not experimentally localized in retrieved evidence. (skovran2019lanthanidesinmethylotrophy pages 6-8)
Caveats / open gaps:
- Direct DNA binding targets (operator motifs), phosphorylation kinetics, and direct MxbM biochemical mechanism are not established in the retrieved sources; treat these as unresolved and avoid over-specific mechanistic claims. (skovran2019lanthanidesinmethylotrophy pages 6-8)
References
(chistoserdova2003methylotrophyinmethylobacterium pages 2-3): Ludmila Chistoserdova, Sung-Wei Chen, Alla Lapidus, and Mary E. Lidstrom. Methylotrophy in methylobacterium extorquens am1 from a genomic point of view. Journal of Bacteriology, 185:2980-2987, May 2003. URL: https://doi.org/10.1128/jb.185.10.2980-2987.2003, doi:10.1128/jb.185.10.2980-2987.2003. This article has 402 citations and is from a peer-reviewed journal.
(skovran2019lanthanidesinmethylotrophy pages 6-8): Elizabeth Skovran, Charumathi Raghuraman, and Norma Cecilia Martinez-Gomez. Lanthanides in methylotrophy. Current issues in molecular biology, 33:101-116, Jan 2019. URL: https://doi.org/10.21775/cimb.033.101, doi:10.21775/cimb.033.101. This article has 49 citations.
(vu2016lanthanidedependentregulationof pages 6-9): Huong N. Vu, Gabriel A. Subuyuj, Srividhya Vijayakumar, Nathan M. Good, N. Cecilia Martinez-Gomez, and Elizabeth Skovran. Lanthanide-dependent regulation of methanol oxidation systems in methylobacterium extorquens am1 and their contribution to methanol growth. Journal of Bacteriology, 198:1250-1259, Apr 2016. URL: https://doi.org/10.1128/jb.00937-15, doi:10.1128/jb.00937-15. This article has 227 citations and is from a peer-reviewed journal.
(chu2016xoxfactsas pages 9-12): Frances Chu and Mary E. Lidstrom. Xoxf acts as the predominant methanol dehydrogenase in the type i methanotroph methylomicrobium buryatense. Journal of Bacteriology, 198:1317-1325, Apr 2016. URL: https://doi.org/10.1128/jb.00959-15, doi:10.1128/jb.00959-15. This article has 194 citations and is from a peer-reviewed journal.
(vu2016lanthanidedependentregulationof pages 31-40): Huong N. Vu, Gabriel A. Subuyuj, Srividhya Vijayakumar, Nathan M. Good, N. Cecilia Martinez-Gomez, and Elizabeth Skovran. Lanthanide-dependent regulation of methanol oxidation systems in methylobacterium extorquens am1 and their contribution to methanol growth. Journal of Bacteriology, 198:1250-1259, Apr 2016. URL: https://doi.org/10.1128/jb.00937-15, doi:10.1128/jb.00937-15. This article has 227 citations and is from a peer-reviewed journal.
(tani2023metabolismlinkedmethylotaxissensors pages 1-2): Akio Tani, Sachiko Masuda, Yoshiko Fujitani, Toshiki Iga, Yuuki Haruna, Shiho Kikuchi, Wang Shuaile, Haoxin Lv, Shiori Katayama, Hiroya Yurimoto, Yasuyoshi Sakai, and Junichi Kato. Metabolism-linked methylotaxis sensors responsible for plant colonization in methylobacterium aquaticum strain 22a. Frontiers in Microbiology, Oct 2023. URL: https://doi.org/10.3389/fmicb.2023.1258452, doi:10.3389/fmicb.2023.1258452. This article has 13 citations and is from a peer-reviewed journal.
(mondal2024bioprospectsofpink pages 14-15): Priyajit Mondal, Dhritishree Ghosh, Madhupa Seth, and Subhra Kanti Mukhopadhyay. Bioprospects of pink pigmented facultative methylotrophs (ppfms). Arab Gulf Journal of Scientific Research, 42:1849-1863, Mar 2024. URL: https://doi.org/10.1108/agjsr-03-2023-0127, doi:10.1108/agjsr-03-2023-0127. This article has 8 citations and is from a peer-reviewed journal.
(selvamani2020engineeringofrecombinant pages 1-3): Vidhya Selvamani, Irisappan Ganesh, Sowon Chae, Murali kannan Maruthamuthu, and Soon Ho Hong. Engineering of recombinant escherichia coli towards methanol sensing using methylobacterium extroquens two-component systems. ArXiv, 48:24-31, Mar 2020. URL: https://doi.org/10.4014/mbl.1908.08009, doi:10.4014/mbl.1908.08009. This article has 3 citations.
(selvamani2020engineeringofrecombinant pages 5-8): Vidhya Selvamani, Irisappan Ganesh, Sowon Chae, Murali kannan Maruthamuthu, and Soon Ho Hong. Engineering of recombinant escherichia coli towards methanol sensing using methylobacterium extroquens two-component systems. ArXiv, 48:24-31, Mar 2020. URL: https://doi.org/10.4014/mbl.1908.08009, doi:10.4014/mbl.1908.08009. This article has 3 citations.
(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 92 citations and is from a peer-reviewed journal.
(skovran2019lanthanidesinmethylotrophy pages 1-2): Elizabeth Skovran, Charumathi Raghuraman, and Norma Cecilia Martinez-Gomez. Lanthanides in methylotrophy. Current issues in molecular biology, 33:101-116, Jan 2019. URL: https://doi.org/10.21775/cimb.033.101, doi:10.21775/cimb.033.101. This article has 49 citations.
(groom2019amutagenicscreen pages 1-2): 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.