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  The orphan histidine protein kinase SgmT is a c-di-GMP receptor and regulates composition of the extracellular matrix together with the orphan DNA binding response regulator DigR in Myxococcus xanthus

Petters, T., Zhang, X., Nesper, J., Treuner-Lange, A., Gomez-Santos, N., Hoppert, M., et al. (2012). The orphan histidine protein kinase SgmT is a c-di-GMP receptor and regulates composition of the extracellular matrix together with the orphan DNA binding response regulator DigR in Myxococcus xanthus. Molecular Microbiology, 84(1), 147-165. doi:10.1111/j.1365-2958.2012.08015.x.

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Datensatz-Permalink: https://hdl.handle.net/21.11116/0000-0007-C0FB-5 Versions-Permalink: https://hdl.handle.net/21.11116/0000-000D-B9E6-F
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 Urheber:
Petters, T.1, Autor           
Zhang, X., Autor
Nesper, J., Autor
Treuner-Lange, A.1, Autor           
Gomez-Santos, N.1, Autor           
Hoppert, M., Autor
Jenal, U., Autor
Sogaard-Andersen, L.1, Autor           
Affiliations:
1Bacterial Adaption and Differentiation, Department of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266305              

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 Zusammenfassung: In Myxococcus xanthus the extracellular matrix is essential for type IV pili-dependent motility and starvation-induced fruiting body formation. Proteins of two-component systems including the orphan DNA binding response regulator DigR are essential in regulating the composition of the extracellular matrix. We identify the orphan hybrid histidine kinase SgmT as the partner kinase of DigR. In addition to kinase and receiver domains, SgmT consists of an N-terminal GAF domain and a C-terminal GGDEF domain. The GAF domain is the primary sensor domain. The GGDEF domain binds the second messenger bis-(3'-5')-cyclic-dimeric-GMP (c-di-GMP) and functions as a c-di-GMP receptor to spatially sequester SgmT. We identify the DigR binding site in the promoter of the fibA gene, which encodes an abundant extracellular matrix metalloprotease. Whole-genome expression profiling experiments in combination with the identified DigR binding site allowed the identification of the DigR regulon and suggests that SgmT/DigR regulates the expression of genes for secreted proteins and enzymes involved in secondary metabolite synthesis. We suggest that SgmT/DigR regulates extracellular matrix composition and that SgmT activity is regulated by two sensor domains with ligand binding to the GAF domain resulting in SgmT activation and c-di-GMP binding to the GGDEF domain resulting in spatial sequestration of SgmT.

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Sprache(n): eng - English
 Datum: 2012-04
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: eDoc: 635464
ISI: 000302013500012
DOI: 10.1111/j.1365-2958.2012.08015.x
 Art des Abschluß: -

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Titel: Molecular Microbiology
  Alternativer Titel : Mol. Microbiol.
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: MALDEN : WILEY-BLACKWELL
Seiten: - Band / Heft: 84 (1) Artikelnummer: - Start- / Endseite: 147 - 165 Identifikator: ISSN: 0950-382X