Commichau, Fabian M.

[["dc.bibliographiccitation.firstpage","1287"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Environmental Microbiology"],["dc.bibliographiccitation.lastpage","1305"],["dc.bibliographiccitation.volume","21"],["dc.contributor.author","Wicke, Dennis"],["dc.contributor.author","Schulz, Lisa M."],["dc.contributor.author","Lentes, Sabine"],["dc.contributor.author","Scholz, Patricia"],["dc.contributor.author","Poehlein, Anja"],["dc.contributor.author","Gibhardt, Johannes"],["dc.contributor.author","Daniel, Rolf"],["dc.contributor.author","Ischebeck, Till"],["dc.contributor.author","Commichau, Fabian M."],["dc.date.accessioned","2021-06-01T10:47:09Z"],["dc.date.available","2021-06-01T10:47:09Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1111/1462-2920.14534"],["dc.identifier.eissn","1462-2920"],["dc.identifier.issn","1462-2912"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/85504"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-425"],["dc.relation.eissn","1462-2920"],["dc.relation.issn","1462-2912"],["dc.title","Identification of the first glyphosate transporter by genomic adaptation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["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.issue","19"],["dc.bibliographiccitation.journal","Applied and Environmental Microbiology"],["dc.bibliographiccitation.volume","84"],["dc.contributor.author","Djouiai, Bahar"],["dc.contributor.author","Thwaite, Joanne E."],["dc.contributor.author","Laws, Thomas R."],["dc.contributor.author","Commichau, Fabian M."],["dc.contributor.author","Setlow, Barbara"],["dc.contributor.author","Setlow, Peter"],["dc.contributor.author","Moeller, Ralf"],["dc.contributor.editor","Schaffner, Donald W."],["dc.date.accessioned","2020-12-10T18:36:51Z"],["dc.date.available","2020-12-10T18:36:51Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1128/AEM.01604-18"],["dc.identifier.eissn","1098-5336"],["dc.identifier.issn","0099-2240"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/76760"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Role of DNA Repair and Protective Components in Bacillus subtilis Spore Resistance to Inactivation by 400-nm-Wavelength Blue Light"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["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","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.journal","Frontiers in Microbiology"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Cortesão, Marta"],["dc.contributor.author","Fuchs, Felix M."],["dc.contributor.author","Commichau, Fabian M."],["dc.contributor.author","Eichenberger, Patrick"],["dc.contributor.author","Schuerger, Andrew C."],["dc.contributor.author","Nicholson, Wayne L."],["dc.contributor.author","Setlow, Peter"],["dc.contributor.author","Moeller, Ralf"],["dc.date.accessioned","2020-12-10T18:44:27Z"],["dc.date.available","2020-12-10T18:44:27Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.3389/fmicb.2019.00333"],["dc.identifier.eissn","1664-302X"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/78458"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Bacillus subtilis Spore Resistance to Simulated Mars Surface Conditions"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","29"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Trends in Biotechnology"],["dc.bibliographiccitation.lastpage","37"],["dc.bibliographiccitation.volume","37"],["dc.contributor.author","Rosenberg, Jonathan"],["dc.contributor.author","Commichau, Fabian M."],["dc.date.accessioned","2020-12-10T15:21:34Z"],["dc.date.available","2020-12-10T15:21:34Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1016/j.tibtech.2018.08.001"],["dc.identifier.issn","0167-7799"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/73075"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Harnessing Underground Metabolism for Pathway Development"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","156"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Environmental Microbiology"],["dc.bibliographiccitation.lastpage","168"],["dc.bibliographiccitation.volume","20"],["dc.contributor.author","Rosenberg, Jonathan"],["dc.contributor.author","Yeak, KahYen C."],["dc.contributor.author","Commichau, Fabian M."],["dc.date.accessioned","2020-12-10T18:26:32Z"],["dc.date.available","2020-12-10T18:26:32Z"],["dc.date.issued","2017"],["dc.identifier.doi","10.1111/1462-2920.13950"],["dc.identifier.issn","1462-2912"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/76109"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","A two-step evolutionary process establishes a non-native vitamin B6 pathway in Bacillus subtilis"],["dc.title.alternative","Vitamin B6 pathway by evolution"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2341"],["dc.bibliographiccitation.journal","Microbiology"],["dc.bibliographiccitation.lastpage","2351"],["dc.bibliographiccitation.volume","160"],["dc.contributor.author","Juhas, Mario"],["dc.contributor.author","Reuss, Daniel R."],["dc.contributor.author","Zhu, Bingyao"],["dc.contributor.author","Commichau, Fabian M."],["dc.date.accessioned","2018-11-07T09:32:47Z"],["dc.date.available","2018-11-07T09:32:47Z"],["dc.date.issued","2014"],["dc.description.abstract","Investigation of essential genes, besides contributing to understanding the fundamental principles of life, has numerous practical applications. Essential genes can be exploited as building blocks of a tightly controlled cell 'chassis'. Bacillus subtilis and Escherichia coli K-12 are both well-characterized model bacteria used as hosts for a plethora of biotechnological applications. Determination of the essential genes that constitute the B. subtilis and E coli minimal genomes is therefore of the highest importance. Recent advances have led to the modification of the original B. subtilis and E. coli essential gene sets identified 10 years ago. Furthermore, significant progress has been made in the area of genome minimization of both model bacteria. This review provides an update, with particular emphasis on the current essential gene sets and their comparison with the original gene sets identified 10 years ago. Special attention is focused on the genome reduction analyses in B. subtilis and E. coli and the construction of minimal cell factories for industrial applications."],["dc.identifier.doi","10.1099/mic.0.079376-0"],["dc.identifier.isi","000347021200001"],["dc.identifier.pmid","25092907"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/31823"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Soc General Microbiology"],["dc.relation.issn","1350-0872"],["dc.title","Bacillus subtilis and Escherichia coli essential genes and minimal cell factories after one decade of genome engineering"],["dc.type","review"],["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"]]