Commichau, Fabian M.

[["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.issue","10"],["dc.bibliographiccitation.journal","Journal of Bacteriology"],["dc.bibliographiccitation.volume","201"],["dc.contributor.author","Quintana, Ingrid M."],["dc.contributor.author","Gibhardt, Johannes"],["dc.contributor.author","Turdiev, Asan"],["dc.contributor.author","Hammer, Elke"],["dc.contributor.author","Commichau, Fabian M."],["dc.contributor.author","Lee, Vincent T."],["dc.contributor.author","Magni, Christian"],["dc.contributor.author","Stülke, Jörg"],["dc.contributor.editor","Stock, Ann M."],["dc.date.accessioned","2020-12-10T18:37:01Z"],["dc.date.available","2020-12-10T18:37:01Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1128/JB.00028-19"],["dc.identifier.eissn","1098-5530"],["dc.identifier.issn","0021-9193"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/76816"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","The KupA and KupB Proteins of Lactococcus lactis IL1403 Are Novel c-di-AMP Receptor Proteins Responsible for Potassium Uptake"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1350"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Molecular & Cellular Proteomics"],["dc.bibliographiccitation.lastpage","1360"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Commichau, Fabian M."],["dc.contributor.author","Rothe, Fabian M."],["dc.contributor.author","Herzberg, Christina"],["dc.contributor.author","Wagner, Eva M."],["dc.contributor.author","Hellwig, Daniel"],["dc.contributor.author","Lehnik-Habrink, Martin"],["dc.contributor.author","Hammer, Elke"],["dc.contributor.author","Voelker, Uwe"],["dc.contributor.author","Stuelke, Joerg"],["dc.date.accessioned","2018-11-07T08:29:31Z"],["dc.date.available","2018-11-07T08:29:31Z"],["dc.date.issued","2009"],["dc.description.abstract","Glycolysis is one of the most important metabolic pathways in heterotrophic organisms. Several genes encoding glycolytic enzymes are essential in many bacteria even under conditions when neither glycolytic nor gluconeogenic activities are required. In this study, a screening for in vivo interaction partners of glycolytic enzymes of the soil bacterium Bacillus subtilis was used to provide a rationale for essentiality of glycolytic enzymes. Glycolytic enzymes proved to be in close contact with several other proteins, among them a high proportion of essential proteins. Among these essential interaction partners, other glycolytic enzymes were most prominent. Two-hybrid studies confirmed interactions of phosphofructokinase with phosphoglyceromutase and enolase. Such a complex of glycolytic enzymes might allow direct substrate channeling of glycolytic intermediates. Moreover we found associations of glycolytic enzymes with several proteins known or suspected to be involved in RNA processing and degradation. One of these proteins, Rny (YmdA), which has so far not been functionally characterized, is required for the processing of the mRNA of the glycolytic gapA operon. Two-hybrid analyses confirmed the interactions between the glycolytic enzymes phosphofructokinase and enolase and the enzymes involved in RNA processing, RNase J1, Rny, and polynucleotide phosphorylase. Moreover RNase J1 interacts with its homologue RNase J2. We suggest that this complex of mRNA processing and glycolytic enzymes is the B. subtilis equivalent of the RNA degradosome. Our findings suggest that the functional interaction of glycolytic enzymes with essential proteins may be the reason why they are indispensable. Molecular & Cellular Proteomics 8: 1350-1360, 2009."],["dc.identifier.doi","10.1074/mcp.M800546-MCP200"],["dc.identifier.isi","000266904900015"],["dc.identifier.pmid","19193632"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/16674"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Biochemistry Molecular Biology Inc"],["dc.relation.issn","1535-9476"],["dc.title","Novel Activities of Glycolytic Enzymes 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","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","3379"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Environmental Microbiology"],["dc.bibliographiccitation.lastpage","3390"],["dc.bibliographiccitation.volume","17"],["dc.contributor.author","Stannek, Lorena"],["dc.contributor.author","Thiele, Martin J."],["dc.contributor.author","Ischebeck, Till"],["dc.contributor.author","Gunka, Katrin"],["dc.contributor.author","Hammer, Elke"],["dc.contributor.author","Voelker, Uwe"],["dc.contributor.author","Commichau, Fabian M."],["dc.date.accessioned","2018-11-07T09:52:29Z"],["dc.date.available","2018-11-07T09:52:29Z"],["dc.date.issued","2015"],["dc.description.abstract","In the Gram-positive bacterium, Bacillus subtilis glutamate is synthesized by the glutamine synthetase and the glutamate synthase (GOGAT). During growth with carbon sources that exert carbon catabolite repression, the rocG glutamate dehydrogenase (GDH) gene is repressed and the transcription factor GltC activates the expression of the GOGAT encoding gltAB genes. In the presence of amino acids of the glutamate family, the GDH RocG is synthesized and the enzyme prevents GltC from binding to DNA. The dual control of glutamate biosynthesis allows the efficient utilization of the available nutrients. Here we provide genetic and biochemical evidence that, like RocG, also the paralogous GDH GudB can inhibit the transcription factor GltC, thereby controlling glutamate biosynthesis. Contradictory previous observations show that high level of GDH activity does not result in permanent inhibition of GltC. By controlling the intracellular levels of glutamate through feeding with exogenous arginine, we observed that the GDH-dependent control of GltC and thus expression of the gltAB genes inversely correlates with the glutamate pool. These results suggest that the B.subtilisGDHs RocG and GudB in fact act as glutamate sensors. In conclusion, the GDH-mediated control of glutamate biosynthesis seems to depend on the intracellular glutamate concentration."],["dc.identifier.doi","10.1111/1462-2920.12813"],["dc.identifier.isi","000361000500022"],["dc.identifier.pmid","25711804"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/36136"],["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","Evidence for synergistic control of glutamate biosynthesis by glutamate dehydrogenases and glutamate in Bacillus subtilis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]