2.50
Hdl Handle:
http://hdl.handle.net/10033/97535
Title:
Intrinsic thermal sensing controls proteolysis of Yersinia virulence regulator RovA.
Authors:
Herbst, Katharina; Bujara, Matthias; Heroven, Ann Kathrin; Opitz, Wiebke; Weichert, Martin; Zimmermann, Ariane; Dersch, Petra
Abstract:
Pathogens, which alternate between environmental reservoirs and a mammalian host, frequently use thermal sensing devices to adjust virulence gene expression. Here, we identify the Yersinia virulence regulator RovA as a protein thermometer. Thermal shifts encountered upon host entry lead to a reversible conformational change of the autoactivator, which reduces its DNA-binding functions and renders it more susceptible for proteolysis. Cooperative binding of RovA to its target promoters is significantly reduced at 37 degrees C, indicating that temperature control of rovA transcription is primarily based on the autoregulatory loop. Thermally induced reduction of DNA-binding is accompanied by an enhanced degradation of RovA, primarily by the Lon protease. This process is also subject to growth phase control. Studies with modified/chimeric RovA proteins indicate that amino acid residues in the vicinity of the central DNA-binding domain are important for proteolytic susceptibility. Our results establish RovA as an intrinsic temperature-sensing protein in which thermally induced conformational changes interfere with DNA-binding capacity, and secondarily render RovA susceptible to proteolytic degradation.
Affiliation:
Institut für Mikrobiologie, Technische Universität Braunschweig, Germany.
Citation:
Intrinsic thermal sensing controls proteolysis of Yersinia virulence regulator RovA. 2009, 5 (5):e1000435 PLoS Pathog.
Journal:
PLoS pathogens
Issue Date:
May-2009
URI:
http://hdl.handle.net/10033/97535
DOI:
10.1371/journal.ppat.1000435
PubMed ID:
19468295
Type:
Article
Language:
en
ISSN:
1553-7374
Appears in Collections:
publications of the department of molecular Infectionbiology (MIBI)

Full metadata record

DC FieldValue Language
dc.contributor.authorHerbst, Katharinaen
dc.contributor.authorBujara, Matthiasen
dc.contributor.authorHeroven, Ann Kathrinen
dc.contributor.authorOpitz, Wiebkeen
dc.contributor.authorWeichert, Martinen
dc.contributor.authorZimmermann, Arianeen
dc.contributor.authorDersch, Petraen
dc.date.accessioned2010-04-28T08:00:19Z-
dc.date.available2010-04-28T08:00:19Z-
dc.date.issued2009-05-
dc.identifier.citationIntrinsic thermal sensing controls proteolysis of Yersinia virulence regulator RovA. 2009, 5 (5):e1000435 PLoS Pathog.en
dc.identifier.issn1553-7374-
dc.identifier.pmid19468295-
dc.identifier.doi10.1371/journal.ppat.1000435-
dc.identifier.urihttp://hdl.handle.net/10033/97535-
dc.description.abstractPathogens, which alternate between environmental reservoirs and a mammalian host, frequently use thermal sensing devices to adjust virulence gene expression. Here, we identify the Yersinia virulence regulator RovA as a protein thermometer. Thermal shifts encountered upon host entry lead to a reversible conformational change of the autoactivator, which reduces its DNA-binding functions and renders it more susceptible for proteolysis. Cooperative binding of RovA to its target promoters is significantly reduced at 37 degrees C, indicating that temperature control of rovA transcription is primarily based on the autoregulatory loop. Thermally induced reduction of DNA-binding is accompanied by an enhanced degradation of RovA, primarily by the Lon protease. This process is also subject to growth phase control. Studies with modified/chimeric RovA proteins indicate that amino acid residues in the vicinity of the central DNA-binding domain are important for proteolytic susceptibility. Our results establish RovA as an intrinsic temperature-sensing protein in which thermally induced conformational changes interfere with DNA-binding capacity, and secondarily render RovA susceptible to proteolytic degradation.en
dc.language.isoenen
dc.titleIntrinsic thermal sensing controls proteolysis of Yersinia virulence regulator RovA.en
dc.typeArticleen
dc.contributor.departmentInstitut für Mikrobiologie, Technische Universität Braunschweig, Germany.en
dc.identifier.journalPLoS pathogensen
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