Stülke, Jörg

[["dc.bibliographiccitation.firstpage","e01373-20"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Antimicrobial Agents and Chemotherapy"],["dc.bibliographiccitation.volume","65"],["dc.contributor.author","Senges, Christoph H. R."],["dc.contributor.author","Stepanek, Jennifer J."],["dc.contributor.author","Wenzel, Michaela"],["dc.contributor.author","Raatschen, Nadja"],["dc.contributor.author","Ay, Ümran"],["dc.contributor.author","Märtens, Yvonne"],["dc.contributor.author","Prochnow, Pascal"],["dc.contributor.author","Vázquez Hernández, Melissa"],["dc.contributor.author","Yayci, Abdulkadir"],["dc.contributor.author","Schubert, Britta"],["dc.contributor.author","Janzing, Niklas B. M."],["dc.contributor.author","Warmuth, Helen L."],["dc.contributor.author","Kozik, Martin"],["dc.contributor.author","Bongard, Jens"],["dc.contributor.author","Alumasa, John N."],["dc.contributor.author","Albada, Bauke"],["dc.contributor.author","Penkova, Maya"],["dc.contributor.author","Lukežič, Tadeja"],["dc.contributor.author","Sorto, Nohemy A."],["dc.contributor.author","Lorenz, Nicole"],["dc.contributor.author","Miller, Reece G."],["dc.contributor.author","Zhu, Bingyao"],["dc.contributor.author","Benda, Martin"],["dc.contributor.author","Stülke, Jörg"],["dc.contributor.author","Schäkermann, Sina"],["dc.contributor.author","Leichert, Lars I."],["dc.contributor.author","Scheinpflug, Kathi"],["dc.contributor.author","Brötz-Oesterhelt, Heike"],["dc.contributor.author","Hertweck, Christian"],["dc.contributor.author","Shaw, Jared T."],["dc.contributor.author","Petković, Hrvoje"],["dc.contributor.author","Brunel, Jean M."],["dc.contributor.author","Keiler, Kenneth C."],["dc.contributor.author","Metzler-Nolte, Nils"],["dc.contributor.author","Bandow, Julia E."],["dc.date.accessioned","2021-04-14T08:30:00Z"],["dc.date.available","2021-04-14T08:30:00Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1128/AAC.01373-20"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/83066"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation.eissn","1098-6596"],["dc.relation.issn","0066-4804"],["dc.title","Comparison of Proteomic Responses as Global Approach to Antibiotic Mechanism of Action Elucidation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","102144"],["dc.bibliographiccitation.journal","Journal of Biological Chemistry"],["dc.contributor.author","Heidemann, Jana L."],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Krüger, Larissa"],["dc.contributor.author","Wicke, Dennis"],["dc.contributor.author","Vinhoven, Liza"],["dc.contributor.author","Linden, Andreas"],["dc.contributor.author","Dickmanns, Achim"],["dc.contributor.author","Stülke, Jörg"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Ficner, Ralf"],["dc.date.accessioned","2022-07-01T07:35:47Z"],["dc.date.available","2022-07-01T07:35:47Z"],["dc.date.issued","2022"],["dc.identifier.doi","10.1016/j.jbc.2022.102144"],["dc.identifier.pii","S0021925822005865"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/112267"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-581"],["dc.relation.issn","0021-9258"],["dc.title","Structural basis for c-di-AMP-dependent regulation of the bacterial stringent response by receptor protein DarB"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","701"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Environmental Microbiology"],["dc.bibliographiccitation.lastpage","717"],["dc.bibliographiccitation.volume","16"],["dc.contributor.author","Zaprasis, Adrienne"],["dc.contributor.author","Hoffmann, Tamara"],["dc.contributor.author","Wuensche, Guido"],["dc.contributor.author","Florez, Lope A."],["dc.contributor.author","Stuelke, Joerg"],["dc.contributor.author","Bremer, Erhard"],["dc.date.accessioned","2018-11-07T09:42:49Z"],["dc.date.available","2018-11-07T09:42:49Z"],["dc.date.issued","2014"],["dc.description.abstract","The gamma-glutamyl-phosphate reductase (ProA) interlinks both the anabolic and osmostress adaptive proline biosynthetic routes of Bacillus subtilis. Because no paralogous protein to ProA exists in this microorganism, proA mutants should exhibit a tight proline auxotrophic growth phenotype. Contrary to expectations, proA mutants formed microcolonies on agar plates lacking proline and faster growing Pro(+) suppressor mutants arose. These mutants carried alterations in the rocR-rocDEF region encoding enzymes of the arginine degradation pathway and its transcriptional activator RocR. They were of two types: (i) mutants carrying single amino acid substitutions in RocR resulting in partial inducer-independent variants and (ii) mutants carrying single base-pair changes in the vicinity of the SigL/Sig-54-dependent -12/-24 class rocDEF promoter that activate a cryptic SigA-type promoter. Consequently, enhanced rocDEF transcription should lead to increased cellular amounts of the RocD ornithine aminotransferase, an enzyme that synthesizes the same reaction product as ProA, gamma-glutamic-semialdehyde/delta-1-pyrroline-5-carboxylate. This compound can be enzymatically converted into proline. The Pro(+) suppressors also exhibited a new regulatory pattern by allowing enhanced rocDEF transcription in response to proline availability when ammonium is present. Our work provides an example how flexibly bacteria can genetically develop routes to bypass constraints imposed on their biosynthetic networks and evolve new regulatory mechanisms."],["dc.identifier.doi","10.1111/1462-2920.12193"],["dc.identifier.isi","000332085400008"],["dc.identifier.pmid","23869754"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/34045"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","1462-2920"],["dc.relation.issn","1462-2912"],["dc.title","Mutational activation of the RocR activator and of a cryptic rocDEF promoter bypass loss of the initial steps of proline biosynthesis 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","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","136"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Archives of Microbiology"],["dc.bibliographiccitation.lastpage","146"],["dc.bibliographiccitation.volume","185"],["dc.contributor.author","Blencke, Hans-Matti"],["dc.contributor.author","Reif, I."],["dc.contributor.author","Commichau, Fabian M."],["dc.contributor.author","Detsch, C."],["dc.contributor.author","Wacker, I."],["dc.contributor.author","Ludwig, H."],["dc.contributor.author","Stulke, J."],["dc.date.accessioned","2018-11-07T10:09:35Z"],["dc.date.available","2018-11-07T10:09:35Z"],["dc.date.issued","2006"],["dc.description.abstract","The tricarboxylic acid (TCA) cycle is one of the major routes of carbon catabolism in Bacillus subtilis. The syntheses of the enzymes performing the initial reactions of the cycle, citrate synthase, and aconitase, are synergistically repressed by rapidly metabolizable carbon sources and glutamine. This regulation involves the general transcription factor CcpA and the specific repressor CcpC. In this study, we analyzed the expression and intracellular localization of CcpC. The synthesis of citrate, the effector of CcpC, requires acetyl-CoA. This metabolite is located at a branching point in metabolism. It can be converted to acetate in overflow metabolism or to citrate. Manipulations of the fate of acetyl-CoA revealed that efficient citrate synthesis is required for the expression of the citB gene encoding aconitase and that control of the two pathways utilizing acetyl-CoA converges in the control of citrate synthesis for the induction of the TCA cycle. The citrate pool seems also to be controlled by arginine catabolism. The presence of arginine results in a severe CcpC-dependent repression of citB. In addition to regulators involved in sensing the carbon status of the cell, the pleiotropic nitrogen-related transcription factor, TnrA, activates citB transcription in the absence of glutamine."],["dc.identifier.doi","10.1007/s00203-005-0078-0"],["dc.identifier.isi","000235245800007"],["dc.identifier.pmid","16395550"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/39680"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.issn","0302-8933"],["dc.title","Regulation of citB expression in Bacillus subtilis: integration of multiple metabolic signals in the citrate pool and by the general nitrogen regulatory system"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","6939"],["dc.bibliographiccitation.issue","24"],["dc.bibliographiccitation.journal","Journal of Bacteriology"],["dc.bibliographiccitation.lastpage","6949"],["dc.bibliographiccitation.volume","193"],["dc.contributor.author","Meyer, Frederik M."],["dc.contributor.author","Jules, Matthieu"],["dc.contributor.author","Mehne, Felix M. P."],["dc.contributor.author","Le Coq, Dominique"],["dc.contributor.author","Landmann, Jens J."],["dc.contributor.author","Goerke, Boris"],["dc.contributor.author","Aymerich, Stephane"],["dc.contributor.author","Stuelke, Joerg"],["dc.date.accessioned","2018-11-07T08:49:24Z"],["dc.date.available","2018-11-07T08:49:24Z"],["dc.date.issued","2011"],["dc.description.abstract","Most organisms can choose their preferred carbon source from a mixture of nutrients. This process is called carbon catabolite repression. The Gram-positive bacterium Bacillus subtilis uses glucose as the preferred source of carbon and energy. Glucose-mediated catabolite repression is caused by binding of the CcpA transcription factor to the promoter regions of catabolic operons. CcpA binds DNA upon interaction with its cofactors HPr(Ser-P) and Crh(Ser-P). The formation of the cofactors is catalyzed by the metabolite-activated HPr kinase/ phosphorylase. Recently, it has been shown that malate is a second preferred carbon source for B. subtilis that also causes catabolite repression. In this work, we addressed the mechanism by which malate causes catabolite repression. Genetic analyses revealed that malate-dependent catabolite repression requires CcpA and its cofactors. Moreover, we demonstrate that HPr(Ser-P) is present in malate-grown cells and that CcpA and HPr interact in vivo in the presence of glucose or malate but not in the absence of a repressing carbon source. The formation of the cofactor HPr(Ser-P) could be attributed to the concentrations of ATP and fructose 1,6-bisphosphate in cells growing with malate. Both metabolites are available at concentrations that are sufficient to stimulate HPr kinase activity. The adaptation of cells to environmental changes requires dynamic metabolic and regulatory adjustments. The repression strength of target promoters was similar to that observed in steady-state growth conditions, although it took somewhat longer to reach the second steady-state of expression when cells were shifted to malate."],["dc.identifier.doi","10.1128/JB.06197-11"],["dc.identifier.isi","000297810500016"],["dc.identifier.pmid","22001508"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/21449"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Microbiology"],["dc.relation.issn","0021-9193"],["dc.title","Malate-Mediated Carbon Catabolite Repression in Bacillus subtilis Involves the HPrK/CcpA Pathway"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","9605"],["dc.bibliographiccitation.issue","24"],["dc.bibliographiccitation.journal","Journal of Biological Chemistry"],["dc.bibliographiccitation.lastpage","9614"],["dc.bibliographiccitation.volume","294"],["dc.contributor.author","Gundlach, Jan"],["dc.contributor.author","Krüger, Larissa"],["dc.contributor.author","Herzberg, Christina"],["dc.contributor.author","Turdiev, Asan"],["dc.contributor.author","Poehlein, Anja"],["dc.contributor.author","Tascón, Igor"],["dc.contributor.author","Weiss, Martin"],["dc.contributor.author","Hertel, Dietrich"],["dc.contributor.author","Daniel, Rolf"],["dc.contributor.author","Hänelt, Inga"],["dc.contributor.author","Lee, Vincent T."],["dc.contributor.author","Stülke, Jörg"],["dc.date.accessioned","2020-12-10T18:12:59Z"],["dc.date.available","2020-12-10T18:12:59Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1074/jbc.RA119.008774"],["dc.identifier.eissn","1083-351X"],["dc.identifier.issn","0021-9258"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/74548"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Sustained sensing in potassium homeostasis: Cyclic di-AMP controls potassium uptake by KimA at the levels of expression and activity"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","18"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Metabolic Engineering"],["dc.bibliographiccitation.lastpage","27"],["dc.bibliographiccitation.volume","13"],["dc.contributor.author","Meyer, Frederik M."],["dc.contributor.author","Gerwig, Jan"],["dc.contributor.author","Hammer, Elke"],["dc.contributor.author","Herzberg, Christina"],["dc.contributor.author","Commichau, Fabian M."],["dc.contributor.author","Voelker, Uwe"],["dc.contributor.author","Stuelke, Joerg"],["dc.date.accessioned","2018-11-07T09:01:42Z"],["dc.date.available","2018-11-07T09:01:42Z"],["dc.date.issued","2011"],["dc.description.abstract","The majority of all proteins of a living cell is active in complexes rather than in an isolated way. These protein-protein interactions are of high relevance for many biological functions. In addition to many well established protein complexes an increasing number of protein-protein interactions, which form rather transient complexes has recently been discovered. The formation of such complexes seems to be a common feature especially for metabolic pathways. In the Gram-positive model organism Bacillus subtilis, we identified a protein complex of three citric acid cycle enzymes. This complex consists of the citrate synthase, the isocitrate dehydrogenase, and the malate dehydrogenase. Moreover, fumarase and aconitase interact with malate dehydrogenase and with each other. These five enzymes catalyze sequential reaction of the TCA cycle. Thus, this interaction might be important for a direct transfer of intermediates of the TCA cycle and thus for elevated metabolic fluxes via substrate channeling. In addition, we discovered a link between the TCA cycle and gluconeogenesis through a flexible interaction of two proteins: the association between the malate dehydrogenase and phosphoenolpyruvate carboxykinase is directly controlled by the metabolic flux. The phosphoenolpyruvate carboxykinase links the TCA cycle with gluconeogenesis and is essential for B. subtilis growing on gluconeogenic carbon sources. Only under gluconeogenic growth conditions an interaction of these two proteins is detectable and disappears under glycolytic growth conditions. (C) 2010 Elsevier Inc. All rights reserved."],["dc.identifier.doi","10.1016/j.ymben.2010.10.001"],["dc.identifier.isi","000285651100003"],["dc.identifier.pmid","20933603"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/24494"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Academic Press Inc Elsevier Science"],["dc.relation.issn","1096-7176"],["dc.title","Physical interactions between tricarboxylic acid cycle enzymes in Bacillus subtilis: Evidence for a metabolon"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","165"],["dc.bibliographiccitation.issue","1-3"],["dc.bibliographiccitation.journal","Journal of Molecular Microbiology and Biotechnology"],["dc.bibliographiccitation.lastpage","171"],["dc.bibliographiccitation.volume","13"],["dc.contributor.author","Singh, Kalpana D."],["dc.contributor.author","Halbedel, Sven"],["dc.contributor.author","Goerke, Boris"],["dc.contributor.author","Stuelke, Joerg"],["dc.date.accessioned","2018-11-07T11:06:54Z"],["dc.date.available","2018-11-07T11:06:54Z"],["dc.date.issued","2007"],["dc.description.abstract","In the Gram-positive bacterium Bacillus subtilis as well as in other firmicutes, the HPr protein of the phosphotransferase system (PTS) has two distinct phosphorylation sites, His-15 and Ser-46. These sites are phosphorylated by the Enzyme I of the PTS and by the ATP-dependent HPr kinase/phosphorylase, respectively. As a result, the phosphorylation state of HPr reflects the nutrient supply of the cell and is in turn involved in several responses at the levels of transport activity and expression of catabolic genes. Most important, HPr( SerP) serves as a cofactor for the pleiotropic transcription regulator CcpA. In addition to the proteins that phosphorylate HPr, those that are involved in the dephosphorylation are important in controlling the overall HPr phosphorylation state and the resulting regulatory and physiological outputs. In this study, we found that in addition to the phosphorylase activity of the HPr kinase/phosphorylase, the serine/threonine protein phosphatase PrpC uses HPr(Ser-P) as a target. Copyright (c) 2007 S. Karger AG, Basel."],["dc.identifier.doi","10.1159/000103608"],["dc.identifier.isi","000248808400018"],["dc.identifier.pmid","17693724"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/52423"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Karger"],["dc.relation.issn","1464-1801"],["dc.title","Control of the phosphorylation state of the HPr protein of the phosphotransferase system in Bacillus subtilis: Implication of the protein phosphatase PrpC"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1103"],["dc.bibliographiccitation.issue","6072"],["dc.bibliographiccitation.journal","Science"],["dc.bibliographiccitation.lastpage","1106"],["dc.bibliographiccitation.volume","335"],["dc.contributor.author","Nicolas, Pierre"],["dc.contributor.author","Maeder, Ulrike"],["dc.contributor.author","Dervyn, Etienne"],["dc.contributor.author","Rochat, Tatiana"],["dc.contributor.author","Leduc, Aurelie"],["dc.contributor.author","Pigeonneau, Nathalie"],["dc.contributor.author","Bidnenko, Elena"],["dc.contributor.author","Marchadier, Elodie"],["dc.contributor.author","Hoebeke, Mark"],["dc.contributor.author","Aymerich, Stephane"],["dc.contributor.author","Becher, Doerte"],["dc.contributor.author","Bisicchia, Paola"],["dc.contributor.author","Botella, Eric"],["dc.contributor.author","Delumeau, Olivier"],["dc.contributor.author","Doherty, Geoff"],["dc.contributor.author","Denham, Emma L."],["dc.contributor.author","Fogg, Mark J."],["dc.contributor.author","Fromion, Vincent"],["dc.contributor.author","Goelzer, Anne"],["dc.contributor.author","Hansen, Annette"],["dc.contributor.author","Haertig, Elisabeth"],["dc.contributor.author","Harwood, Colin R."],["dc.contributor.author","Homuth, Georg"],["dc.contributor.author","Jarmer, Hanne"],["dc.contributor.author","Jules, Matthieu"],["dc.contributor.author","Klipp, Edda"],["dc.contributor.author","Le Chat, Ludovic"],["dc.contributor.author","Lecointe, Francois"],["dc.contributor.author","Lewis, Peter"],["dc.contributor.author","Liebermeister, Wolfram"],["dc.contributor.author","March, Anika"],["dc.contributor.author","Mars, Ruben A. T."],["dc.contributor.author","Nannapaneni, Priyanka"],["dc.contributor.author","Noone, David"],["dc.contributor.author","Pohl, Susanne"],["dc.contributor.author","Rinn, Bernd"],["dc.contributor.author","Ruegheimer, Frank"],["dc.contributor.author","Sappa, Praveen Kumar"],["dc.contributor.author","Samson, Franck"],["dc.contributor.author","Schaffer, Marc"],["dc.contributor.author","Schwikowski, Benno"],["dc.contributor.author","Steil, Leif"],["dc.contributor.author","Stuelke, Joerg"],["dc.contributor.author","Wiegert, Thomas"],["dc.contributor.author","Devine, Kevin M."],["dc.contributor.author","Wilkinson, Anthony J."],["dc.contributor.author","van Dijl, Jan Maarten"],["dc.contributor.author","Hecker, Michael"],["dc.contributor.author","Voelker, Uwe"],["dc.contributor.author","Bessieres, Philippe"],["dc.contributor.author","Noirot, Philippe"],["dc.date.accessioned","2018-11-07T09:12:26Z"],["dc.date.available","2018-11-07T09:12:26Z"],["dc.date.issued","2012"],["dc.description.abstract","Bacteria adapt to environmental stimuli by adjusting their transcriptomes in a complex manner, the full potential of which has yet to be established for any individual bacterial species. Here, we report the transcriptomes of Bacillus subtilis exposed to a wide range of environmental and nutritional conditions that the organism might encounter in nature. We comprehensively mapped transcription units (TUs) and grouped 2935 promoters into regulons controlled by various RNA polymerase sigma factors, accounting for similar to 66% of the observed variance in transcriptional activity. This global classification of promoters and detailed description of TUs revealed that a large proportion of the detected antisense RNAs arose from potentially spurious transcription initiation by alternative sigma factors and from imperfect control of transcription termination."],["dc.identifier.doi","10.1126/science.1206848"],["dc.identifier.isi","000300931100048"],["dc.identifier.pmid","22383849"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/26944"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Assoc Advancement Science"],["dc.relation.issn","0036-8075"],["dc.title","Condition-Dependent Transcriptome Reveals High-Level Regulatory Architecture in Bacillus subtilis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]