Stülke, Jörg

[["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","175"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Trends in Microbiology"],["dc.bibliographiccitation.lastpage","185"],["dc.bibliographiccitation.volume","26"],["dc.contributor.author","Commichau, Fabian M."],["dc.contributor.author","Gibhardt, Johannes"],["dc.contributor.author","Halbedel, Sven"],["dc.contributor.author","Gundlach, Jan"],["dc.contributor.author","Stülke, Jörg"],["dc.date.accessioned","2020-12-10T15:21:36Z"],["dc.date.available","2020-12-10T15:21:36Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1016/j.tim.2017.09.003"],["dc.identifier.issn","0966-842X"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/73083"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","A Delicate Connection: c-di-AMP Affects Cell Integrity by Controlling Osmolyte Transport"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["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.firstpage","42"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Molecular Microbiology"],["dc.bibliographiccitation.lastpage","54"],["dc.bibliographiccitation.volume","100"],["dc.contributor.author","Grosshennig, Stephanie"],["dc.contributor.author","Ischebeck, Till"],["dc.contributor.author","Gibhardt, Johannes"],["dc.contributor.author","Busse, Julia"],["dc.contributor.author","Feussner, Ivo"],["dc.contributor.author","Stuelke, Joerg"],["dc.date.accessioned","2018-11-07T10:16:28Z"],["dc.date.available","2018-11-07T10:16:28Z"],["dc.date.issued","2016"],["dc.description.abstract","Mycoplasma pneumoniae is a human pathogen causing atypical pneumonia with a minimalized and highly streamlined genome. So far, hydrogen peroxide production, cytadherence, and the ADP-ribosylating CARDS toxin have been identified as pathogenicity determinants. We have studied haemolysis caused by M. pneumoniae, and discovered that hydrogen peroxide is responsible for the oxidation of heme, but not for lysis of erythrocytes. This feature could be attributed to hydrogen sulfide, a compound that has previously not been identified as virulence factor in lung pathogens. Indeed, we observed hydrogen sulfide production by M. pneumoniae. The search for a hydrogen sulfide-producing enzyme identified HapE, a protein with similarity to cysteine desulfurases. In contrast to typical cysteine desulfurases, HapE is a bifunctional enzyme: it has both the cysteine desulfurase activity to produce alanine and the cysteine desulfhydrase activity to produce pyruvate and hydrogen sulfide. Experiments with purified HapE showed that the enzymatic activity of the protein is responsible for haemolysis, demonstrating that HapE is a novel potential virulence factor of M. pneumoniae."],["dc.identifier.doi","10.1111/mmi.13300"],["dc.identifier.isi","000373155200004"],["dc.identifier.pmid","26711628"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/41045"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","1365-2958"],["dc.relation.issn","0950-382X"],["dc.title","Hydrogen sulfide is a novel potential virulence factor of Mycoplasma pneumoniae: characterization of the unusual cysteine desulfurase/desulfhydrase HapE"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]