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Stülke, Jörg
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Preferred name
Stülke, Jörg
Official Name
Stülke, Jörg
Alternative Name
Stuelke, Joerg
Stuelke, J.
Stülke, J.
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2017Journal Article [["dc.bibliographiccitation.artnumber","1328"],["dc.bibliographiccitation.journal","Frontiers in microbiology"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Blötz, Cedric"],["dc.contributor.author","Treffon, Katrin"],["dc.contributor.author","Kaever, Volkhard"],["dc.contributor.author","Schwede, Frank"],["dc.contributor.author","Hammer, Elke"],["dc.contributor.author","Stülke, Jörg"],["dc.date.accessioned","2019-07-09T11:43:38Z"],["dc.date.available","2019-07-09T11:43:38Z"],["dc.date.issued","2017"],["dc.description.abstract","Bacteria often use cyclic dinucleotides as second messengers for signal transduction. While the classical molecule c-di-GMP is involved in lifestyle selection, the functions of the more recently discovered signaling nucleotide cyclic di-AMP are less defined. For many Gram-positive bacteria, c-di-AMP is essential for growth suggesting its involvement in a key cellular function. We have analyzed c-di-AMP signaling in the genome-reduced pathogenic bacterium Mycoplasma pneumoniae. Our results demonstrate that these bacteria produce c-di-AMP, and we could identify the diadenylate cyclase CdaM (MPN244). This enzyme is the founding member of a novel family of diadenylate cyclases. Of two potential c-di-AMP degrading phosphodiesterases, only PdeM (MPN549) is active in c-di-AMP degradation, whereas NrnA (MPN140) was reported to degrade short oligoribonucleotides. As observed in other bacteria, both the c-di-AMP synthesizing and the degrading enzymes are essential for M. pneumoniae suggesting control of a major homeostatic process. To obtain more insights into the nature of this process, we have identified a c-di-AMP-binding protein from M. pneumoniae, KtrC. KtrC is the cytoplasmic regulatory subunit of the low affinity potassium transporter KtrCD. It is established that binding of c-di-AMP inhibits the KtrCD activity resulting in a limitation of potassium uptake. Our results suggest that the control of potassium homeostasis is the essential function of c-di-AMP in M. pneumoniae."],["dc.identifier.doi","10.3389/fmicb.2017.01328"],["dc.identifier.pmid","28751888"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14609"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/58934"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation.issn","1664-302X"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject.ddc","570"],["dc.title","Identification of the Components Involved in Cyclic Di-AMP Signaling in Mycoplasma pneumoniae"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]Details DOI PMID PMC