Stülke, Jörg

[["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","3069"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Journal of biological chemistry"],["dc.bibliographiccitation.lastpage","3080"],["dc.bibliographiccitation.volume","290"],["dc.contributor.author","Gundlach, Jan"],["dc.contributor.author","Dickmanns, Achim"],["dc.contributor.author","Schröder-Tittmann, Kathrin"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Kaesler, Jan"],["dc.contributor.author","Kampf, Jan"],["dc.contributor.author","Herzberg, Christina"],["dc.contributor.author","Hammer, Elke"],["dc.contributor.author","Schwede, Frank"],["dc.contributor.author","Kaever, Volkhard"],["dc.contributor.author","Tittmann, Kai"],["dc.contributor.author","Stülke, Jörg"],["dc.contributor.author","Ficner, Ralf"],["dc.date.accessioned","2017-09-07T11:44:39Z"],["dc.date.available","2017-09-07T11:44:39Z"],["dc.date.issued","2015"],["dc.description.abstract","Background: Cyclic di-AMP is an essential second messenger in eubacteria. Results: The c-di-AMP receptor DarA was identified in B. subtilis. The crystal structure and ITC data revealed the nucleotide specificity of DarA. Conclusion: DarA is a P-II-like protein that undergoes conformational changes upon c-di-AMP binding. Significance: A novel P-II-like protein is involved in c-di-AMP signaling. The cyclic dimeric AMP nucleotide c-di-AMP is an essential second messenger in Bacillus subtilis. We have identified the protein DarA as one of the prominent c-di-AMP receptors in B. subtilis. Crystal structure analysis shows that DarA is highly homologous to P-II signal transducer proteins. In contrast to P-II proteins, the functionally important B- and T-loops are swapped with respect to their size. DarA is a homotrimer that binds three molecules of c-di-AMP, each in a pocket located between two subunits. We demonstrate that DarA is capable to bind c-di-AMP and with lower affinity cyclic GMP-AMP (33-cGAMP) but not c-di-GMP or 23-cGAMP. Consistently the crystal structure shows that within the ligand-binding pocket only one adenine is highly specifically recognized, whereas the pocket for the other adenine appears to be promiscuous. Comparison with a homologous ligand-free DarA structure reveals that c-di-AMP binding is accompanied by conformational changes of both the fold and the position of the B-loop in DarA."],["dc.identifier.doi","10.1074/jbc.M114.619619"],["dc.identifier.gro","3141969"],["dc.identifier.isi","000349310700043"],["dc.identifier.pmid","25433025"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/3090"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Deutsche Forschungsgemeinschaft [HI 291/13-1, SFB860]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1083-351X"],["dc.relation.issn","0021-9258"],["dc.title","Identification, Characterization, and Structure Analysis of the Cyclic di-AMP-binding P-II-like Signal Transduction Protein DarA"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]