Gunka, Katrin

[["dc.bibliographiccitation.firstpage","1036"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Journal of Bacteriology"],["dc.bibliographiccitation.lastpage","1044"],["dc.bibliographiccitation.volume","194"],["dc.contributor.author","Gunka, Katrin"],["dc.contributor.author","Tholen, Stefan"],["dc.contributor.author","Gerwig, Jan"],["dc.contributor.author","Herzberg, Christina"],["dc.contributor.author","Stuelke, Joerg"],["dc.contributor.author","Commichau, Fabian M."],["dc.date.accessioned","2018-11-07T09:13:08Z"],["dc.date.available","2018-11-07T09:13:08Z"],["dc.date.issued","2012"],["dc.description.abstract","Common laboratory strains of Bacillus subtilis encode two glutamate dehydrogenases: the enzymatically active protein RocG and the cryptic enzyme GudB that is inactive due to a duplication of three amino acids in its active center. The inactivation of the rocG gene results in poor growth of the bacteria on complex media due to the accumulation of toxic intermediates. Therefore, rocG mutants readily acquire suppressor mutations that decryptify the gudB gene. This decryptification occurs by a precise deletion of one part of the 9-bp direct repeat that causes the amino acid duplication. This mutation occurs at the extremely high frequency of 10(-4). Mutations affecting the integrity of the direct repeat result in a strong reduction of the mutation frequency; however, the actual sequence of the repeat is not essential. The mutation frequency of gudB was not affected by the position of the gene on the chromosome. When the direct repeat was placed in the completely different context of an artificial promoter, the precise deletion of one part of the repeat was also observed, but the mutation frequency was reduced by 3 orders of magnitude. Thus, transcription of the gudB gene seems to be essential for the high frequency of the appearance of the gudB1 mutation. This idea is supported by the finding that the transcription-repair coupling factor Mfd is required for the decryptification of gudB. The Mfd-mediated coupling of transcription to mutagenesis might be a built-in precaution that facilitates the accumulation of mutations preferentially in transcribed genes."],["dc.identifier.doi","10.1128/JB.06470-11"],["dc.identifier.isi","000300530800015"],["dc.identifier.pmid","22178973"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/27106"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Microbiology"],["dc.relation.issn","0021-9193"],["dc.title","A High-Frequency Mutation in Bacillus subtilis: Requirements for the Decryptification of the gudB Glutamate Dehydrogenase Gene"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","213"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Molecular Microbiology"],["dc.bibliographiccitation.lastpage","224"],["dc.bibliographiccitation.volume","85"],["dc.contributor.author","Gunka, Katrin"],["dc.contributor.author","Commichau, Fabian M."],["dc.date.accessioned","2018-11-07T09:08:37Z"],["dc.date.available","2018-11-07T09:08:37Z"],["dc.date.issued","2012"],["dc.description.abstract","Glutamate, the major amino group donor in anabolism, is synthesized by the combined action of the glutamine synthetase (GS) and the glutamate synthase (GOGAT) in Bacillus subtilis. The glutamate dehydrogenase (GDH) exclusively degrades glutamate. GS and GDH are both trigger enzymes, active in nitrogen metabolism and in controlling gene expression. Feedback-inhibited GS (FBI-GS) controls DNA-binding activities of two transcription factors, the repressor GlnR and TnrA, the global regulator of nitrogen metabolism. FBI-GS binds to and activates GlnR. This protein complex inhibits GS formation and thus glutamine synthesis. Moreover, FBI-GS inhibits DNA-binding activity of TnrA. Glutamate biosynthesis, the reaction linking carbon with nitrogen metabolism, is controlled by GDH. Together with glutamate GDH inhibits GltC, the transcription factor that activates expression of the GOGAT genes. Thus, GS and GDH control glutamine and glutamate synthesis, respectively, depending on the nitrogen status of the cell. B. subtilis lacking a functional GDH show a severe growth defect. Interestingly, the growth defect is suppressed by the rapid activation of an inactive GDH. Thus, maintenance of glutamate homeostasis is crucial for cellular vitality. This review covers the recent work on the complex control of glutamine and glutamate metabolism in the Gram-positive model organism B. subtilis."],["dc.description.sponsorship","Fonds der Chemischen Industrie"],["dc.identifier.doi","10.1111/j.1365-2958.2012.08105.x"],["dc.identifier.isi","000306140300003"],["dc.identifier.pmid","22625175"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/26073"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","0950-382X"],["dc.title","Control of glutamate homeostasis in Bacillus subtilis: a complex interplay between ammonium assimilation, glutamate biosynthesis and degradation"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","682"],["dc.bibliographiccitation.journal","Microbiology"],["dc.bibliographiccitation.lastpage","691"],["dc.bibliographiccitation.volume","160"],["dc.contributor.author","Gerwig, Jan"],["dc.contributor.author","Kiley, Taryn B."],["dc.contributor.author","Gunka, Katrin"],["dc.contributor.author","Stanley-Wall, Nicola"],["dc.contributor.author","Stuelkel, Joerg"],["dc.date.accessioned","2018-11-07T09:41:31Z"],["dc.date.available","2018-11-07T09:41:31Z"],["dc.date.issued","2014"],["dc.description.abstract","The Gram-positive soil bacterium Bacillus subtilis is able to choose between motile and sessile lifestyles. The sessile way of life, also referred to as biofilm, depends on the formation of an extracellular polysaccharide matrix and some extracellular proteins. Moreover, a significant proportion of cells in a biofilm form spores. The first two genes of the 15-gene operon for extracellular polysaccharide synthesis, epsA and epsB, encode a putative transmembrane modulator protein and a putative protein tyrosine kinase, respectively, with similarity to the TkmA/PtkA modulator/kinase couple. Here we show that the putative kinase EpsB is required for the formation of structured biofilms. However, an epsB mutant is still able to form biofilms. As shown previously, a ptkA mutant is also partially defective in biofilm formation, but this defect is related to spore formation in the biofilm. The absence of both kinases resulted in a complete loss of biofilm formation. Thus, EpsB and PtkA fulfil complementary functions in biofilm formation. The activity of bacterial protein tyrosine kinases depends on their interaction with modulator proteins. Our results demonstrate the specific interaction between the putative kinase EpsB and its modulator protein EpsA and suggest that EpsB activity is stimulated by its modulator EpsA."],["dc.identifier.doi","10.1099/mic.0.074971-0"],["dc.identifier.isi","000338603400004"],["dc.identifier.pmid","24493247"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/33752"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Soc General Microbiology"],["dc.relation.issn","1350-0872"],["dc.title","The protein tyrosine kinases EpsB and PtkA differentially affect biofilm formation in Bacillus subtilis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2004"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Journal of Biological Chemistry"],["dc.bibliographiccitation.lastpage","2017"],["dc.bibliographiccitation.volume","288"],["dc.contributor.author","Mehne, Felix M. P."],["dc.contributor.author","Gunka, Katrin"],["dc.contributor.author","Eilers, Hinnerk"],["dc.contributor.author","Herzberg, Christina"],["dc.contributor.author","Kaever, Volkhard"],["dc.contributor.author","Stuelke, Joerg"],["dc.date.accessioned","2018-11-07T09:29:07Z"],["dc.date.available","2018-11-07T09:29:07Z"],["dc.date.issued","2013"],["dc.description.abstract","The genome of the Gram-positive soil bacterium Bacillus subtilis encodes three potential diadenylate cyclases that may synthesize the signaling nucleotide cyclic di-AMP (c-di-AMP). These enzymes are expressed under different conditions in different cell compartments, and they localize to distinct positions in the cell. Here we demonstrate the diadenylate cyclase activity of the so far uncharacterized enzymes CdaA (previously known as YbbP) and CdaS (YojJ). Our work confirms that c-di-AMP is essential for the growth of B. subtilis and shows that an excess of the molecule is also harmful for the bacteria. Several lines of evidence suggest that the diadenylate cyclase CdaA is part of the conserved essential cda-glm module involved in cell wall metabolism. In contrast, the CdaS enzyme seems to provide c-di-AMP for spores. Accumulation of large amounts of c-di-AMP impairs the growth of B. subtilis and results in the formation of aberrant curly cells. This phenotype can be partially suppressed by elevated concentrations of magnesium. These observations suggest that c-di-AMP interferes with the peptidoglycan synthesis machinery. The activity of the diadenylate cyclases is controlled by distinct molecular mechanisms. CdaA is stimulated by a regulatory interaction with the CdaR (YbbR) protein. In contrast, the activity of CdaS seems to be intrinsically restricted, and a single amino acid substitution is sufficient to drastically increase the activity of the enzyme. Taken together, our results support the idea of an important role for c-di-AMP in B. subtilis and suggest that the levels of the nucleotide have to be tightly controlled."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft"],["dc.identifier.doi","10.1074/jbc.M112.395491"],["dc.identifier.isi","000313751400052"],["dc.identifier.pmid","23192352"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/30943"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Biochemistry Molecular Biology Inc"],["dc.relation.issn","0021-9258"],["dc.title","Cyclic Di-AMP Homeostasis in Bacillus subtilis BOTH LACK AND HIGH LEVEL ACCUMULATION OF THE NUCLEOTIDE ARE DETRIMENTAL FOR CELL GROWTH"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3557"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Journal of Bacteriology"],["dc.bibliographiccitation.lastpage","3564"],["dc.bibliographiccitation.volume","190"],["dc.contributor.author","Commichau, Fabian M."],["dc.contributor.author","Gunka, Katrin"],["dc.contributor.author","Landmann, Jens J."],["dc.contributor.author","Stuelke, Joerg"],["dc.date.accessioned","2018-11-07T11:15:36Z"],["dc.date.available","2018-11-07T11:15:36Z"],["dc.date.issued","2008"],["dc.description.abstract","Glutamate is a central metabolite in all organisms since it provides the link between carbon and nitrogen metabolism. In Bacillus subtilis, glutamate is synthesized exclusively by the glutamate synthase, and it can be degraded by the glutamate dehydrogenase. In B. subtilis, the major glutamate dehydrogenase RocG is expressed only in the presence of arginine, and the bacteria are unable to utilize glutamate as the only carbon source. In addition to rocG, a second cryptic gene (gudB) encodes an inactive glutamate dehydrogenase. Mutations in rocG result in the rapid accumulation of gudB1 suppressor mutations that code for an active enzyme. In this work, we analyzed the physiological significance of this constellation of genes and enzymes involved in glutamate metabolism. We found that the weak expression of rocG in the absence of the inducer arginine is limiting for glutamate utilization. Moreover, we addressed the potential ability of the active glutamate dehydrogenases of B. subtilis to synthesize glutamate. Both RocG and GudB1 were unable to catalyze the anabolic reaction, most probably because of their very high K-m values for ammonium. In contrast, the Escherichia coli glutamate dehydrogenase is able to produce glutamate even in the background of a B. subtilis cell. B. subtilis responds to any mutation that interferes with glutamate metabolism with the rapid accumulation of extragenic or intragenic suppressor mutations, bringing the glutamate supply into balance. Similarly, with the presence of a cryptic gene, the system can flexibly respond to changes in the external glutamate supply by the selection of mutations."],["dc.identifier.doi","10.1128/JB.00099-08"],["dc.identifier.isi","000255622500015"],["dc.identifier.pmid","18326565"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/54401"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Microbiology"],["dc.relation.issn","0021-9193"],["dc.title","Glutamate metabolism in Bacillus subtilis: Gene expression and enzyme activities evolved to avoid futile cycles and to allow rapid responses to perturbations of the system"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e51196"],["dc.bibliographiccitation.issue","83"],["dc.bibliographiccitation.journal","Journal of Visualized Experiments"],["dc.contributor.author","Stannek, Lorena"],["dc.contributor.author","Egelkamp, Richard"],["dc.contributor.author","Gunka, Katrin"],["dc.contributor.author","Commichau, Fabian M."],["dc.date.accessioned","2018-11-07T09:45:24Z"],["dc.date.available","2018-11-07T09:45:24Z"],["dc.date.issued","2014"],["dc.description.abstract","Many microorganisms such as bacteria proliferate extremely fast and the populations may reach high cell densities. Small fractions of cells in a population always have accumulated mutations that are either detrimental or beneficial for the cell. If the fitness effect of a mutation provides the subpopulation with a strong selective growth advantage, the individuals of this subpopulation may rapidly outcompete and even completely eliminate their immediate fellows. Thus, small genetic changes and selection-driven accumulation of cells that have acquired beneficial mutations may lead to a complete shift of the genotype of a cell population. Here we present a procedure to monitor the rapid clonal expansion and elimination of beneficial and detrimental mutations, respectively, in a bacterial cell population over time by cocultivation of fluorescently labeled individuals of the Gram-positive model bacterium Bacillus subtilis. The method is easy to perform and very illustrative to display intraspecies competition among the individuals in a bacterial cell population."],["dc.identifier.doi","10.3791/51196"],["dc.identifier.isi","000348513500062"],["dc.identifier.pmid","24473333"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/34610"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Journal Of Visualized Experiments"],["dc.relation.issn","1940-087X"],["dc.title","Monitoring Intraspecies Competition in a Bacterial Cell Population by Cocultivation of Fluorescently Labelled Strains"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","815"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Journal of Molecular Biology"],["dc.bibliographiccitation.lastpage","827"],["dc.bibliographiccitation.volume","400"],["dc.contributor.author","Gunka, Katrin"],["dc.contributor.author","Newman, Joseph A."],["dc.contributor.author","Commichau, Fabian M."],["dc.contributor.author","Herzberg, Christina"],["dc.contributor.author","Rodrigues, Cecilia"],["dc.contributor.author","Hewitt, Lorraine"],["dc.contributor.author","Lewis, Richard J."],["dc.contributor.author","Stuelke, Joerg"],["dc.date.accessioned","2018-11-07T08:41:18Z"],["dc.date.available","2018-11-07T08:41:18Z"],["dc.date.issued","2010"],["dc.description.abstract","Any signal transduction requires communication between a sensory component and an effector. Some enzymes engage in signal perception and transduction, as well as in catalysis, and these proteins are known as \"trigger\" enzymes. In this report, we detail the trigger properties of RocG, the glutamate dehydrogenase of Bacillus subtilis. RocG not only deaminates the key metabolite glutamate to form alpha-ketoglutarate but also interacts directly with GltC, a LysR-type transcription factor that regulates glutamate biosynthesis from alpha-ketoglutarate, thus linking the two metabolic pathways. We have isolated mutants of RocG that separate the two functions. Several mutations resulted in permanent inactivation of GltC as long as a source of glutamate was present. These RocG proteins have lost their ability to catabolize glutamate due to a strongly reduced affinity for glutamate. The second class of mutants is exemplified by the replacement of aspartate residue 122 by asparagine. This mutant protein has retained enzymatic activity but has lost the ability to control the activity of GltC. Crystal structures of glutamate dehydrogenases that permit a molecular explanation of the properties of the various mutants are presented. Specifically, we may propose that D122N replacement affects the surface of RocG. Our data provide evidence for a correlation between the enzymatic activity of RocG and its ability to inactivate GltC, and thus give insights into the mechanism that couples the enzymatic activity of a trigger enzyme to its regulatory function. (C) 2010 Elsevier Ltd. All rights reserved."],["dc.identifier.doi","10.1016/j.jmb.2010.05.055"],["dc.identifier.isi","000280652300014"],["dc.identifier.pmid","20630473"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/19436"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Academic Press Ltd- Elsevier Science Ltd"],["dc.relation.issn","0022-2836"],["dc.title","Functional Dissection of a Trigger Enzyme: Mutations of the Bacillus subtilis Glutamate Dehydrogenase RocG That Affect Differentially Its Catalytic Activity and Regulatory Properties"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","515"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Journal of Bacteriology"],["dc.bibliographiccitation.lastpage","526"],["dc.bibliographiccitation.volume","196"],["dc.contributor.author","Zaprasis, Adrienne"],["dc.contributor.author","Hoffmann, Tamara"],["dc.contributor.author","Stannek, Lorena"],["dc.contributor.author","Gunka, Katrin"],["dc.contributor.author","Commichau, Fabian M."],["dc.contributor.author","Bremer, Erhard"],["dc.date.accessioned","2018-11-07T09:44:02Z"],["dc.date.available","2018-11-07T09:44:02Z"],["dc.date.issued","2014"],["dc.description.abstract","PutP and OpuE serve as proline transporters when this imino acid is used by Bacillus subtilis as a nutrient or as an osmostress protectant, respectively. The simultaneous inactivation of the PutP and OpuE systems still allows the utilization of proline as a nutrient. This growth phenotype pointed to the presence of a third proline transport system in B. subtilis. We took advantage of the sensitivity of a putP opuE double mutant to the toxic proline analog 3,4-dehydro-DL-proline (DHP) to identify this additional proline uptake system. DHP-resistant mutants were selected and found to be defective in the use of proline as a nutrient. Whole-genome resequencing of one of these strains provided the lead that the inactivation of the gamma-aminobutyrate (GABA) transporter GabP was responsible for these phenotypes. DNA sequencing of the gabP gene in 14 additionally analyzed DHP-resistant strains confirmed this finding. Consistently, each of the DHP-resistant mutants was defective not only in the use of proline as a nutrient but also in the use of GABA as a nitrogen source. The same phenotype resulted from the targeted deletion of the gabP gene in a putP opuE mutant strain. Hence, the GabP carrier not only serves as an uptake system for GABA but also functions as the third proline transporter of B. subtilis. Uptake studies with radiolabeled GABA and proline confirmed this conclusion and provided information on the kinetic parameters of the GabP carrier for both of these substrates."],["dc.identifier.doi","10.1128/JB.01128-13"],["dc.identifier.isi","000332625000001"],["dc.identifier.pmid","24142252"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/34307"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Microbiology"],["dc.relation.issn","1098-5530"],["dc.relation.issn","0021-9193"],["dc.title","The gamma-Aminobutyrate Permease GabP Serves as the Third Proline Transporter of Bacillus subtilis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","354"],["dc.bibliographiccitation.journal","Microbiology"],["dc.bibliographiccitation.lastpage","361"],["dc.bibliographiccitation.volume","161"],["dc.contributor.author","Dormeyer, Miriam"],["dc.contributor.author","Egelkamp, Richard"],["dc.contributor.author","Thiele, Martin J."],["dc.contributor.author","Hammer, Elke"],["dc.contributor.author","Gunka, Katrin"],["dc.contributor.author","Stannek, Lorena"],["dc.contributor.author","Voelker, Uwe"],["dc.contributor.author","Commichau, Fabian M."],["dc.date.accessioned","2018-11-07T10:01:11Z"],["dc.date.available","2018-11-07T10:01:11Z"],["dc.date.issued","2015"],["dc.description.abstract","Bacillus subtilis is a Gram-positive bacterium that is easy to manipulate genetically. Several methods for genome engineering have been developed that helped to extend our understanding of how the B. subtilis cell operates. Consequently, the bacterium has become one of the best-studied organisms. B. subtilis has also been engineered for industrial applications. Moreover, great progress has been achieved in promoter engineering to improve the performance of production strains. To expand the toolbox for engineering B. subtilis, we have constructed a system for the inducer-free activation of gene expression. The system relies on spontaneous mutational activation of a cryptic promoter and selection-driven enrichment of bacteria harbouring the mutated promoter. The synthetic promoter is cryptic due to a perfect direct repeat, separating the binding motifs of the RNA polymerase housekeeping sigma factor. The promoter can be fused to genes for industrial applications and to a growth-promoting gene that, upon mutational activation of the promoter, allows enrichment of the engineered bacteria due to a selective growth advantage."],["dc.identifier.doi","10.1099/mic.0.000001"],["dc.identifier.isi","000356647800012"],["dc.identifier.pmid","25473090"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/37961"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.issn","1350-0872"],["dc.title","novel engineering tool in the Bacillus subtilis toolbox: inducer-free activation of gene expression by selection-driven promoter decryptification"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","5997"],["dc.bibliographiccitation.issue","21"],["dc.bibliographiccitation.journal","Journal of Bacteriology"],["dc.bibliographiccitation.lastpage","6007"],["dc.bibliographiccitation.volume","193"],["dc.contributor.author","Diethmaier, Christine"],["dc.contributor.author","Pietack, Nico"],["dc.contributor.author","Gunka, Katrin"],["dc.contributor.author","Wrede, Christoph"],["dc.contributor.author","Lehnik-Habrink, Martin"],["dc.contributor.author","Herzberg, Christina"],["dc.contributor.author","Huebner, Sebastian"],["dc.contributor.author","Stuelke, Joerg"],["dc.date.accessioned","2018-11-07T08:50:29Z"],["dc.date.available","2018-11-07T08:50:29Z"],["dc.date.issued","2011"],["dc.description.abstract","Cells of Bacillus subtilis can either be motile or sessile, depending on the expression of mutually exclusive sets of genes that are required for flagellum or biofilm formation, respectively. Both activities are coordinated by the master regulator SinR. We have analyzed the role of the previously uncharacterized ymdB gene for bistable gene expression in B. subtilis. We observed a strong overexpression of the hag gene encoding flagellin and of other genes of the sigma(D)-dependent motility regulon in the ymdB mutant, whereas the two major operons for biofilm formation, tapA-sipW-tasA and epsA-O, were not expressed. As a result, the ymdB mutant is unable to form biofilms. An analysis of the individual cells of a population revealed that the ymdB mutant no longer exhibited bistable behavior; instead, all cells are short and motile. The inability of the ymdB mutant to form biofilms is suppressed by the deletion of the sinR gene encoding the master regulator of biofilm formation, indicating that SinR-dependent repression of biofilm genes cannot be relieved in a ymdB mutant. Our studies demonstrate that lack of expression of SlrR, an antagonist of SinR, is responsible for the observed phenotypes. Overexpression of SlrR suppresses the effects of a ymdB mutation."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft [SFB860]; Fonds der Chemischen Industrie"],["dc.identifier.doi","10.1128/JB.05360-11"],["dc.identifier.isi","000296153400012"],["dc.identifier.pmid","21856853"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/21703"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Microbiology"],["dc.relation.issn","0021-9193"],["dc.title","A Novel Factor Controlling Bistability in Bacillus subtilis: the YmdB Protein Affects Flagellin Expression and Biofilm Formation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]