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.artnumber","1492"],["dc.bibliographiccitation.journal","Frontiers in Microbiology"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Cascante-Estepa, Nora"],["dc.contributor.author","Gunka, Katrin"],["dc.contributor.author","Stuelke, Joerg"],["dc.date.accessioned","2018-11-07T10:08:26Z"],["dc.date.available","2018-11-07T10:08:26Z"],["dc.date.issued","2016"],["dc.description.abstract","In bacteria, the control of mRNA stability is crucial to allow rapid adaptation to changing conditions. In most bacteria, RNA degradation is catalyzed by the RNA degradosome, a protein complex composed of endo- and exoribonucleases, RNA helicases, and accessory proteins. In the Gram-positive model organism Bacillus subtilis, the existence of a RNA degradosome assembled around the membrane-bound endoribonuclease RNase Y has been proposed. Here, we have studied the intracellular localization of the protein that have been implicated in the potential B. subtilis RNA degradosome, i.e., polynucleotide phosphorylase, the exoribonucleases J1 and J2, the DEAD-box RNA helicase CshA, and the glycolytic enzymes enolase and phosphofructokinase. Our data suggests that the bulk of these enzymes is located in the cytoplasm. The RNases J1 and J2 as well as the RNA helicase CshA were mainly localized in the peripheral regions of the cell where also the bulk of messenger RNA is localized. We were able to demonstrate active exclusion of these proteins from the transcribing nucleoid. Taken together, our findings suggest that the interactions of the enzymes involved in RNA degradation in B. subtilis are rather transient."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2016"],["dc.identifier.doi","10.3389/fmicb.2016.01492"],["dc.identifier.isi","000383647300001"],["dc.identifier.pmid","27708634"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13776"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/39460"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Frontiers Media Sa"],["dc.relation.issn","1664-302X"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Localization of Components of the RNA-Degrading Machine in Bacillus subtilis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["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.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.artnumber","5"],["dc.bibliographiccitation.journal","BMC Systems Biology"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Florez, Lope A."],["dc.contributor.author","Gunka, Katrin"],["dc.contributor.author","Polania, Rafael"],["dc.contributor.author","Tholen, Stefan"],["dc.contributor.author","Stuelke, Joerg"],["dc.date.accessioned","2018-11-07T09:00:06Z"],["dc.date.available","2018-11-07T09:00:06Z"],["dc.date.issued","2011"],["dc.description.abstract","Background: Several computational methods exist to suggest rational genetic interventions that improve the productivity of industrial strains. Nonetheless, these methods are less effective to predict possible genetic responses of the strain after the intervention. This problem requires a better understanding of potential alternative metabolic and regulatory pathways able to counteract the targeted intervention. Results: Here we present SPABBATS, an algorithm based on Boolean satisfiability (SAT) that computes alternative metabolic pathways between input and output species in a reconstructed network. The pathways can be constructed iteratively in order of increasing complexity. SPABBATS allows the accumulation of intermediates in the pathways, which permits discovering pathways missed by most traditional pathway analysis methods. In addition, we provide a proof of concept experiment for the validity of the algorithm. We deleted the genes for the glutamate dehydrogenases of the Gram-positive bacterium Bacillus subtilis and isolated suppressor mutant strains able to grow on glutamate as single carbon source. Our SAT approach proposed candidate alternative pathways which were decisive to pinpoint the exact mutation of the suppressor strain. Conclusions: SPABBATS is the first application of SAT techniques to metabolic problems. It is particularly useful for the characterization of metabolic suppressor mutants and can be used in a synthetic biology setting to design new pathways with specific input-output requirements."],["dc.identifier.doi","10.1186/1752-0509-5-5"],["dc.identifier.isi","000286521700001"],["dc.identifier.pmid","21219666"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/7228"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/24070"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Biomed Central Ltd"],["dc.relation.issn","1752-0509"],["dc.rights","CC BY 2.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/2.0"],["dc.title","SPABBATS: A pathway-discovery method based on Boolean satisfiability that facilitates the characterization of suppressor mutants"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["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"]]

[["dc.bibliographiccitation.artnumber","eaal3011"],["dc.bibliographiccitation.issue","475"],["dc.bibliographiccitation.journal","Science Signaling"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Gundlach, Jan"],["dc.contributor.author","Herzberg, Christina"],["dc.contributor.author","Kaever, Volkhard"],["dc.contributor.author","Gunka, Katrin"],["dc.contributor.author","Hoffmann, Tamara"],["dc.contributor.author","Weiss, Martin"],["dc.contributor.author","Gibhardt, Johannes"],["dc.contributor.author","Thuermer, Andrea"],["dc.contributor.author","Hertel, Dietrich"],["dc.contributor.author","Daniel, Rolf"],["dc.contributor.author","Bremer, Erhard"],["dc.contributor.author","Commichau, Fabian M."],["dc.contributor.author","Stulke, Joerg"],["dc.date.accessioned","2018-11-07T10:24:56Z"],["dc.date.available","2018-11-07T10:24:56Z"],["dc.date.issued","2017"],["dc.description.abstract","The second messenger cyclic di-adenosine monophosphate (c-di-AMP) is essential in the Gram-positive model organism Bacillus subtilis and in related pathogenic bacteria. It controls the activity of the conserved ydaO riboswitch and of several proteins involved in potassium (K+) uptake. We found that the YdaO protein was conserved among several different bacteria and provide evidence that YdaO functions as a K+ transporter. Thus, we renamed the gene and protein KimA (K+ importer A). Reporter activity assays indicated that expression beyond the c-di-AMP-responsive riboswitch of the kimA upstream regulatory region occurred only in bacteria grown in medium containing low K+ concentrations. Furthermore, mass spectrometry analysis indicated that c-di-AMP accumulated in bacteria grown in the presence of high K+ concentrations but not in low concentrations. A bacterial strain lacking all genes encoding c-di-AMP-synthesizing enzymes was viable when grown in medium containing low K+ concentrations, but not at higher K+ concentrations unless it acquired suppressor mutations in the gene encoding the cation exporter NhaK. Thus, our results indicated that the control of potassium homeostasis is an essential function of c-di-AMP."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft [SPP1879]"],["dc.identifier.doi","10.1126/scisignal.aal3011"],["dc.identifier.isi","000400128400003"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/42751"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Amer Assoc Advancement Science"],["dc.relation.issn","1937-9145"],["dc.relation.issn","1945-0877"],["dc.title","Control of potassium homeostasis is an essential function of the second messenger cyclic di-AMP 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.artnumber","883"],["dc.bibliographiccitation.journal","Frontiers in Microbiology"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Toedter, Dominik"],["dc.contributor.author","Gunka, Katrin"],["dc.contributor.author","Stuelke, Joerg"],["dc.date.accessioned","2018-11-07T10:23:44Z"],["dc.date.available","2018-11-07T10:23:44Z"],["dc.date.issued","2017"],["dc.description.abstract","In most bacteria, fatty acid biosynthesis is an essential process that must be controlled by the availability of precursors and by the needs of cell division. So far, no mechanisms controlling synthesis of malonyl-coenzyme A (CoA), the committed step in fatty acid synthesis, have been identified in the Gram-positive model bacterium Bacillus subtilis. We have studied the localization and function of two highly expressed proteins of unknown function, YqhY and YloU. Both proteins are members of the conserved and widespread Asp23 family. While the deletion of yloU had no effect, loss of the yqhY gene induced the rapid acquisition of suppressor mutations. The vast majority of these mutations affect subunits of the acetyl-CoA carboxylase (ACCase) complex, the enzyme that catalyzes the formation of malonyl-CoA. Moreover, lack of yqhY is accompanied by the formation of lipophilic clusters in the polar regions of the cells indicating an increased activity of ACCase. Our results suggest that YqhY controls the activity of ACCase and that this control results in inhibition of ACCase activity. Hyperactivity of the enzyme complex in the absence of YqhY does then provoke mutations that cause reduced ACCase activity."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft [SFB860]"],["dc.identifier.doi","10.3389/fmicb.2017.00883"],["dc.identifier.isi","000401692200001"],["dc.identifier.pmid","28579978"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14498"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/42519"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Frontiers Media Sa"],["dc.relation.issn","1664-302X"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","The Highly Conserved Asp23 Family Protein YqhY Plays a Role in Lipid Biosynthesis in Bacillus subtilis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]