The DOI matches its Crossref record.
Genetic control of osmoadaptive glycine betaine synthesis in Bacillus subtilis through the choline-sensing and glycine betaine-responsive GbsR repressor.
Open accessAbstract
Synthesis of the compatible solute glycine betaine confers a considerable degree of osmotic stress tolerance to Bacillus subtilis. This osmoprotectant is produced through the uptake of the precursor choline via the osmotically inducible OpuB and OpuC ABC transporters and a subsequent two-step oxidation process by the GbsB and GbsA enzymes. We characterized a regulatory protein, GbsR, controlling the transcription of both the structural genes for the glycine betaine biosynthetic enzymes (gbsAB) and those for the choline-specific OpuB transporter (opuB) but not of that for the promiscuous OpuC transporter. GbsR acts genetically as a repressor and functions as an intracellular choline sensor. Spectroscopic analysis of the purified GbsR protein showed that it binds the inducer choline with an apparent K(D) (equilibrium dissociation constant) of approximately 165 μM. Based on the X-ray structure of a protein (Mj223) from Methanococcus jannaschii, a homology model for GbsR was derived. Inspection of this GbsR in silico model revealed a possible ligand-binding pocket for choline resembling those of known choline-binding sites present in solute receptors of microbial ABC transporters, e.g., that of the OpuBC ligand-binding protein of the OpuB ABC transporter. GbsR was not only needed to control gbsAB and opuB expression in response to choline availability but also required to genetically tune down glycine betaine production once cellular adjustment to high osmolarity has been achieved. The GbsR regulatory protein from B. subtilis thus records and integrates cellular and environmental signals for both the onset and the repression of the synthesis of the osmoprotectant glycine betaine.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Bacillus subtilis contains three GbsR-type regulatory proteins whose structural genes are positioned either adjacent to the gbsAB operon (gbsR), the opuC operon (opcR/yvbF), or the opuB operon (yvaV).
“Bacillus subtilis contains three GbsR-type regulatory proteins whose structural genes are positioned either adjacent to the gbsAB operon (gbsR), the opuC operon (opcR/yvbF), or the opuB operon (yvaV) (Nau-Wagner et al., 2012; Lee et al., 2013; Ronzheimer et al., 2018; Figure 2B).”
From Two MarR-Type Repressors Balance Precursor Uptake and Glycine Betaine Synthesis in Bacillus subtilis to Provide Cytoprotection Against Sustained Osmotic Stress (2020) · cites this paper as Nau-Wagner et al., 2012
The GbsR and OpcR regulatory proteins jointly repress the activity of the opuB promoter.
“The GbsR and OpcR regulatory proteins jointly repress the activity of the opuB promoter (Nau-Wagner et al., 2012; Lee et al., 2013; Figure 6A).”
From Two MarR-Type Repressors Balance Precursor Uptake and Glycine Betaine Synthesis in Bacillus subtilis to Provide Cytoprotection Against Sustained Osmotic Stress (2020) · cites this paper as Nau-Wagner et al., 2012
The originally proposed GbsR operator for the gbsAB gene cluster by Nau-Wagner et al. (2012) is not correct, as none of the introduced mutations resulted in loss of GbsR-dependent repression of transcription.
“Collectively, these data showed that the originally proposed GbsR operator for the gbsAB gene cluster by Nau-Wagner et al. (2012) is not correct as none of the introduced mutations resulted in loss of GbsR-dependent repression of transcription (Supplementary Table S1).”
From Two MarR-Type Repressors Balance Precursor Uptake and Glycine Betaine Synthesis in Bacillus subtilis to Provide Cytoprotection Against Sustained Osmotic Stress (2020) · cites this paper as Nau-Wagner et al., 2012
The crystal structure of Mj223 can be used to establish in silico models for GbsR-type proteins.
“The crystal structure of the DNA-binding protein Mj223 from Methanococcus jannaschii (PDB accession code: 1ku9) (Ray et al., 2003), a MarR-type protein of unknown function, can be used to establish in silico models for GbsR-type proteins (Nau-Wagner et al., 2012; Hoffmann et al., 2018; Ronzheimer et al., 2018).”
From Two MarR-Type Repressors Balance Precursor Uptake and Glycine Betaine Synthesis in Bacillus subtilis to Provide Cytoprotection Against Sustained Osmotic Stress (2020) · cites this paper as Nau-Wagner et al., 2012
The mechanistic different modes of action of B. subtilis GbsR and OpcR repressors to control gene expression are likely evolutionarily conserved for their orthologs in many members of the genus Bacillus.
“Hence, the data reported here and those published previously (Nau-Wagner et al., 2012; Lee et al., 2013) collectively suggest that the mechanistic different modes of actions of the B. subtilis GbsR and OpcR repressors to control gene expression (Bervoets and Charlier, 2019) are likely evolutionarily conserved for their orthologs present in many members of the genus Bacillus.”
From Two MarR-Type Repressors Balance Precursor Uptake and Glycine Betaine Synthesis in Bacillus subtilis to Provide Cytoprotection Against Sustained Osmotic Stress (2020) · cites this paper as Nau-Wagner et al., 2012
Moderate osmotic up-shocks trigger rapidly enhanced transcription of both opuB and opuC operons.
“Moderate osmotic up-shocks trigger a rapidly enhanced transcription of both operons (Kappes et al., 1999; Hahne et al., 2010; Nau-Wagner et al., 2012; Nicolas et al., 2012; Lee et al., 2013).”
From Two MarR-Type Repressors Balance Precursor Uptake and Glycine Betaine Synthesis in Bacillus subtilis to Provide Cytoprotection Against Sustained Osmotic Stress (2020) · cites this paper as Nau-Wagner et al., 2012
GbsR-mediated control of opuB and gbsAB expression, and its feedback inhibition by intracellular glycine betaine pools, contributes to the physiologically relevant process of adjusting compatible solute uptake.
“Likewise, the GbsR-mediated control of opuB and gbsAB expression, and its feed-back inhibition by intracellular glycine betaine pools (Nau-Wagner et al., 2012) also contributes to this physiologically relevant process.”
From Two MarR-Type Repressors Balance Precursor Uptake and Glycine Betaine Synthesis in Bacillus subtilis to Provide Cytoprotection Against Sustained Osmotic Stress (2020) · cites this paper as Nau-Wagner et al., 2012
YvaV is neither involved in opuB and opuC expression nor required for regulation of the gbsAB glycine betaine synthesis operon.
“It is neither involved in opuB and opuC expression (Figures 6A,B) nor required for the regulation of the gbsAB glycine betaine synthesis operon (Nau-Wagner et al., 2012).”
From Two MarR-Type Repressors Balance Precursor Uptake and Glycine Betaine Synthesis in Bacillus subtilis to Provide Cytoprotection Against Sustained Osmotic Stress (2020) · cites this paper as Nau-Wagner et al., 2012
GbsR and OpcR belong to the same sub-family of MarR-type transcriptional regulators.
“These two amino acid-sequence-related proteins (Nau-Wagner et al., 2012; Lee et al., 2013) belong to the same sub-family of MarR-type transcriptional regulators (Grove, 2017; Ronzheimer et al., 2018).”
From Two MarR-Type Repressors Balance Precursor Uptake and Glycine Betaine Synthesis in Bacillus subtilis to Provide Cytoprotection Against Sustained Osmotic Stress (2020) · cites this paper as Nau-Wagner et al., 2012
A number of buffer conditions significantly improved the stability of the recombinant GbsR-Strep-tag II protein.
“While we were not able to determine a reliable Tm for the GbsR-Strep-tag II resuspended in the buffer mentioned above (Nau-Wagner et al., 2012), a number of buffer conditions lead to a significant improvement in the stability of the recombinant protein (Supplementary Figure S6).”
From Two MarR-Type Repressors Balance Precursor Uptake and Glycine Betaine Synthesis in Bacillus subtilis to Provide Cytoprotection Against Sustained Osmotic Stress (2020) · cites this paper as Nau-Wagner et al., 2012
The inducers (choline and glycine betaine aldehyde, and their arsenic analogs) and effectors (glycine betaine and arsenobetaine) that dictate the DNA-binding properties of GbsR are known.
“While the inducers (choline and glycine betaine aldehyde, and their arsenic analogs) and effectors (glycine betaine and arsenobetaine) that dictate the DNA-binding properties of GbsR are known (Nau-Wagner et al., 2012; Hoffmann et al., 2018), corresponding information for the OpcR repressor is still lacking.”
From Two MarR-Type Repressors Balance Precursor Uptake and Glycine Betaine Synthesis in Bacillus subtilis to Provide Cytoprotection Against Sustained Osmotic Stress (2020) · cites this paper as Nau-Wagner et al., 2012
The interplay of GbsR and OpcR repressor proteins for opuB and opuC transcription and the compatible solute pools in osmotically stressed cells provides B. subtilis with an effective stress-relieving control unit.
“The interplay of the GbsR and OpcR repressor proteins for opuB and opuC transcription (Nau-Wagner et al., 2012; Lee et al., 2013) and the compatible solute pools in osmotically stressed cells (Hoffmann et al., 2013) provides B. subtilis with an effective stress-relieving control unit.”
From Two MarR-Type Repressors Balance Precursor Uptake and Glycine Betaine Synthesis in Bacillus subtilis to Provide Cytoprotection Against Sustained Osmotic Stress (2020) · cites this paper as Nau-Wagner et al., 2012
Citations
Cites
No references could be resolved yet.
Research works printed but not linked: 65
- Aktas, 2011, Choline uptake in Agrobacterium tumefaciens by the high-affinity ChoXWV transporter, J. Bacteriol., 193, 5119, 10.1128/JB.05421-11 · DOI
- Altschul, 1990, Basic local alignment search tool, J. Mol. Biol., 215, 403, 10.1016/S0022-2836(05)80360-2 · DOI · Paper page
- Arnold, 2006, The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling, Bioinformatics, 22, 195, 10.1093/bioinformatics/bti770 · DOI
- Boch, 1994, Osmoregulation in Bacillus subtilis: synthesis of the osmoprotectant glycine betaine from exogenously provided choline, J. Bacteriol., 176, 5364, 10.1128/jb.176.17.5364-5371.1994 · DOI · Paper page
- Boch, 1996, Synthesis of the osmoprotectant glycine betaine in Bacillus subtilis: characterization of the gbsAB genes, J. Bacteriol., 178, 5121, 10.1128/jb.178.17.5121-5129.1996 · DOI · Paper page
- Boch, 1997, Glycine betaine aldehyde dehydrogenase from Bacillus subtilis: characterization of an enzyme required for the synthesis of the osmoprotectant glycine betaine, Arch. Microbiol., 168, 282, 10.1007/s002030050500 · DOI
- Borwankar, 2011, Natural osmolytes remodel the aggregation pathway of mutant huntingtin exon 1, Biochemistry, 50, 2048, 10.1021/bi1018368 · DOI
- Bourot, 2000, Glycine betaine-assisted protein folding in a lysA mutant of Escherichia coli., J. Biol. Chem., 275, 1050, 10.1074/jbc.275.2.1050 · DOI
- Bremer, 2002, Adaptation to changing osmolarity, 385, 10.1128/9781555817992.ch27 · DOI
- Bremer, 2011, A look into the aromatic cage, Environ. Microbiol. Rep., 3, 1
- Bremer, 2000, Coping with osmotic challenges: osmoregulation through accumulation and release of compatible solutes, 79
- Brigulla, 2003, Chill induction of the SigB-dependent general stress response in Bacillus subtilis and its contribution to low-temperature adaptation, J. Bacteriol., 185, 4305, 10.1128/JB.185.15.4305-4314.2003 · DOI
- Brill, 2011, Osmotically controlled synthesis of the compatible solute proline is critical for cellular defense of Bacillus subtilis against high osmolarity, J. Bacteriol., 193, 5335, 10.1128/JB.05490-11 · DOI
- Bult, 1996, Complete genome sequence of the methanogenic archaeon Methanococcus jannaschii., Science, 273, 1058, 10.1126/science.273.5278.1058 · DOI
- Burkhardt, 2009, Synthesis of glycine betaine from choline in the moderate halophile Halobacillus halophilus: co-regulation of two divergent, polycistronic operons, Environ. Microbiol. Rep., 1, 38, 10.1111/j.1758-2229.2008.00001.x · DOI
- Chattopadhyay, 2004, The chemical chaperone proline relieves the thermosensitivity of a dnaK deletion mutant at 42°C, J. Bacteriol., 186, 8149, 10.1128/JB.186.23.8149-8152.2004 · DOI
- Diamant, 2001, Chemical chaperones regulate molecular chaperones in vitro and in cells under combined salt and heat stresses, J. Biol. Chem., 276, 39586, 10.1074/jbc.M103081200 · DOI
- Dougherty, 1996, Cation-pi interactions in chemistry and biology: a new view of benzene, Phe, Tyr, and Trp, Science, 271, 163, 10.1126/science.271.5246.163 · DOI
- Du, 2011, Structures of the substrate-binding protein provide insights into the multiple compatible solute binding specificities of the Bacillus subtilis ABC transporter OpuC, Biochem. J., 436, 283, 10.1042/BJ20102097 · DOI
- Gajiwala, 2000, Winged helix proteins, Curr. Opin. Struct. Biol., 10, 110, 10.1016/S0959-440X(99)00057-3 · DOI
- Glaasker, 1996, Glycine betaine fluxes in Lactobacillus plantarum during osmostasis and hyper- and hypo-osmotic shock, J. Biol. Chem., 271, 10060, 10.1074/jbc.271.17.10060 · DOI
- Gotsche, 1995, Purification and characterization of the phospho-α-(1,1)glucosidase (TreA) of Bacillus subtilis 168, J. Bacteriol., 177, 2721, 10.1128/jb.177.10.2721-2726.1995 · DOI
- Gu, 2008, Characterization of the glycine betaine biosynthetic genes in the moderately halophilic bacterium Halobacillus dabanensis D-8T, Curr. Microbiol., 57, 306, 10.1007/s00284-008-9194-9 · DOI
- Hahne, 2010, A comprehensive proteomics and transcriptomics analysis of Bacillus subtilis salt stress adaptation, J. Bacteriol., 192, 870, 10.1128/JB.01106-09 · DOI · Paper page
- Harwood, 1990, Growth, maintenance and general techniques, 1
- Harwood, 1990, Molecular biological methods for Bacillus
- Haswell, 2011, Mechanosensitive channels: what can they do and how do they do it?, Structure, 19, 1356, 10.1016/j.str.2011.09.005 · DOI
- Helmann, 1995, Compilation and analysis of Bacillus subtilis sigma A-dependent promoter sequences: evidence for extended contact between RNA polymerase and upstream promoter DNA, Nucleic Acids Res., 23, 2351, 10.1093/nar/23.13.2351 · DOI
- Hoffmann, 2008, Responses of Bacillus subtilis to hypotonic challenges: physiological contributions of mechanosensitive channels to cellular survival, Appl. Environ. Microbiol., 74, 2454, 10.1128/AEM.01573-07 · DOI
- Hoffmann, 2011, Protection of Bacillus subtilis against cold stress via compatible-solute acquisition, J. Bacteriol., 193, 1552, 10.1128/JB.01319-10 · DOI
- Holtmann, 2004, Thermoprotection of Bacillus subtilis by exogenously provided glycine betaine and structurally related compatible solutes: involvement of Opu transporters, J. Bacteriol., 186, 1683, 10.1128/JB.186.6.1683-1693.2004 · DOI
- Horn, 2006, Molecular determinants for substrate specificity of the ligand-binding protein OpuAC from Bacillus subtilis for the compatible solutes glycine betaine and proline betaine, J. Mol. Biol., 357, 592, 10.1016/j.jmb.2005.12.085 · DOI
- Huffman, 2002, Prokaryotic transcription regulators: more than just the helix-turn-helix motif, Curr. Opin. Struct. Biol., 12, 98, 10.1016/S0959-440X(02)00295-6 · DOI
- Kappes, 1998, Response of Bacillus subtilis to high osmolarity: uptake of carnitine, crotonobetaine and butyrobetaine via the ABC transport system OpuC, Microbiology, 144, 83, 10.1099/00221287-144-1-83 · DOI
- Kappes, 1996, Three transport systems for the osmoprotectant glycine betaine operate in Bacillus subtilis: characterization of OpuD, J. Bacteriol., 178, 5071, 10.1128/jb.178.17.5071-5079.1996 · DOI
- Kappes, 1999, Two evolutionarily closely related ABC transporters mediate the uptake of choline for synthesis of the osmoprotectant glycine betaine in Bacillus subtilis., Mol. Microbiol., 32, 203, 10.1046/j.1365-2958.1999.01354.x · DOI · Paper page
- Kempf, 1995, OpuA, an osmotically regulated binding protein-dependent transport system for the osmoprotectant glycine betaine in Bacillus subtilis., J. Biol. Chem., 270, 16701, 10.1074/jbc.270.28.16701 · DOI
- Kempf, 1998, Uptake and synthesis of compatible solutes as microbial stress responses to high osmolality environments, Arch. Microbiol., 170, 319, 10.1007/s002030050649 · DOI
- Kimura, 2010, Glycine betaine biosynthesized from glycine provides an osmolyte for cell growth and spore germination during osmotic stress in Myxococcus xanthus., J. Bacteriol., 192, 1467, 10.1128/JB.01118-09 · DOI
- Koo, 1991, Regulation of compatible solute accumulation in Salmonella typhimurium: evidence for a glycine betaine efflux system, J. Gen. Microbiol., 137, 2617, 10.1099/00221287-137-11-2617 · DOI
- Kortstee, 1970, The aerobic decomposition of choline by microorganisms, Arch. Microbiol., 71, 235
- Lamark, 1991, DNA sequence and analysis of the bet genes encoding the osmoregulatory choline-glycine betaine pathway of Escherichia coli., Mol. Microbiol., 5, 1049, 10.1111/j.1365-2958.1991.tb01877.x · DOI
- Lamark, 1992, Efflux of choline and glycine betaine from osmoregulating cells of Escherichia coli., FEMS Microbiol. Lett., 75, 149, 10.1111/j.1574-6968.1992.tb05408.x · DOI
- Miller, 1972, Experiments in molecular genetics
- Nau-Wagner, 1999, High-affinity transport of choline-O-sulfate and its use as a compatible solute in Bacillus subtilis., Appl. Environ. Microbiol., 65, 560, 10.1128/AEM.65.2.560-568.1999 · DOI
- Nyyssöl̈, 2000, Extreme halophiles synthesize betaine from glycine by methylation, J. Biol. Chem., 275, 22196, 10.1074/jbc.M910111199 · DOI
- Oswald, 2008, Crystal structures of the choline/acetylcholine substrate-binding protein ChoX from Sinorhizobium meliloti in the liganded and unliganded-closed states, J. Biol. Chem., 283, 32848, 10.1074/jbc.M806021200 · DOI
- Pittelkow, 2011, The crystal structure of the substrate-binding protein OpuBC from Bacillus subtilis in complex with choline, J. Mol. Biol., 411, 53, 10.1016/j.jmb.2011.05.037 · DOI
- Quaye, 2009, Contribution of flavin covalent linkage with histidine 99 to the reaction catalyzed by choline oxidase, J. Biol. Chem., 284, 16990, 10.1074/jbc.M109.003715 · DOI
- Ray, 2003, X-ray structure of an M. jannaschii DNA-binding protein: implications for antibiotic resistance in S. aureus., Proteins, 50, 170, 10.1002/prot.10272 · DOI · Paper page
- Rosenstein, 1999, The choline-converting pathway in Staphylococcus xylosus C2A: genetic and physiological characterization, J. Bacteriol., 181, 2273, 10.1128/JB.181.7.2273-2278.1999 · DOI
- Schiefner, 2004, Cation-pi interactions as determinants for binding of the compatible solutes glycine betaine and proline betaine by the periplasmic ligand-binding protein ProX from Escherichia coli., J. Biol. Chem., 279, 5588, 10.1074/jbc.M309771200 · DOI
- Smits, 2008, The compatible-solute-binding protein OpuAC from Bacillus subtilis: ligand binding, site-directed mutagenesis, and crystallographic studies, J. Bacteriol., 190, 5663, 10.1128/JB.00346-08 · DOI
- Srivatsan, 2008, High-precision, whole-genome sequencing of laboratory strains facilitates genetic studies, PLoS Genet., 4, e1000139, 10.1371/journal.pgen.1000139 · DOI
- Steil, 2003, Genome-wide transcriptional profiling analysis of adaptation of Bacillus subtilis to high salinity, J. Bacteriol., 185, 6358, 10.1128/JB.185.21.6358-6370.2003 · DOI
- Street, 2010, Osmolyte-induced conformational changes in the Hsp90 molecular chaperone, Protein Sci., 19, 57, 10.1002/pro.282 · DOI
- Thompson, 2000, DbClustal: rapid and reliable global multiple alignments of protein sequences detected by database searches, Nucleic Acids Res., 28, 2919, 10.1093/nar/28.15.2919 · DOI
- Tschapek, 2011, Arg149 is involved in switching the low affinity, open state of the binding protein AfProX into its high affinity, closed state, J. Mol. Biol., 411, 36, 10.1016/j.jmb.2011.05.039 · DOI
- Waditee, 2005, Genes for direct methylation of glycine provide high levels of glycinebetaine and abiotic-stress tolerance in Synechococcus and Arabidopsis., Proc. Natl. Acad. Sci. U. S. A., 102, 1318, 10.1073/pnas.0409017102 · DOI
- Wahome, 2009, Levels and localization of mechanosensitive channel proteins in Bacillus subtilis., Arch. Microbiol., 191, 403, 10.1007/s00203-009-0465-z · DOI
- Whatmore, 1990, The effects of osmotic upshock on the intracellular solute pools of Bacillus subtilis., J. Gen. Microbiol., 136, 2527, 10.1099/00221287-136-12-2527 · DOI · Paper page
- Whatmore, 1990, Determination of turgor pressure in Bacillus subtilis: a possible role for K+ in turgor regulation, J. Gen. Microbiol., 136, 2521, 10.1099/00221287-136-12-2521 · DOI · Paper page
- Wood, 2001, Osmosensing and osmoregulatory compatible solute accumulation by bacteria, Comp. Biochem. Physiol. A Mol. Integr. Physiol., 130, 437, 10.1016/S1095-6433(01)00442-1 · DOI
- Yancey, 2005, Organic osmolytes as compatible, metabolic and counteracting cytoprotectants in high osmolarity and other stresses, J. Exp. Biol., 208, 2819, 10.1242/jeb.01730 · DOI · Paper page
- Ziegler, 2010, The BCCT family of carriers: from physiology to crystal structure, Mol. Microbiol., 78, 13, 10.1111/j.1365-2958.2010.07332.x · DOI
Cited by
Sorted by citations
Management of Osmotic Stress by Bacillus Subtilis: Genetics and Physiology
Hoffmann, T., & Bremer, E. (2016) · Stress and Environmental Regulation of Gene Expression and Adaptation in Bacteria · doi:10.1002/9781119004813.ch63 · Cited by 39
Self-citationWarmbold, B., Ronzheimer, S., Freibert, S.-A., Seubert, A., Hoffmann, T., & Bremer, E. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.01700 · Cited by 17
Self-citationLee, C.-H., Wu, T.-Y., & Shaw, G.-C. (2013) · Microbiology · doi:10.1099/mic.0.067074-0 · Cited by 13
Metadata
- Authors
- Nau-Wagner, G., Opper, D., Rolbetzki, A., Boch, J., Kempf, B., Hoffmann, T., & Bremer, E.
- Affiliations
- Philipps University of Marburg (DE)
- Venue
- Journal of Bacteriology
- Publisher
- American Society for Microbiology
- Published
- 2012-03-09
- Volume
- 194
- Issue
- 10
- Pages
- 2703-2714
- ISSN
- 0021-9193 (ISSN-L)
- PMC
- PMC3347207
- OpenAlex
- W2093759486
- Cited by
- 65
- References
- 0
- Citations by year
- 2026: 7 · 2025: 7 · 2024: 2 · 2023: 2 · 2022: 8 · 2021: 3 · 2020: 5 · 2019: 3 · 2018: 7 · 2017: 3 · 2016: 5 · 2015: 4 · 2014: 3 · 2013: 4 · 2012: 2
- FWCI
- 2.51
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Bacteriology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Microbial Metabolic Engineering and Bioproduction
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Keywords
- osmoadaptation, Bacillus subtilis, choline-binding proteins, transcriptional repression, osmoprotectants, osmolytes, homology modeling, binding pocket, gene expression regulation
- MeSH terms
- Bacillus subtilis, Bacterial Proteins, Base Sequence, Betaine, Binding Sites, Choline, Models, Molecular, Protein Binding, Protein Conformation, Repressor Proteins, Gene Expression Regulation, Bacterial, Genome, Bacterial, Gene Deletion, Feedback, Physiological
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
