Pannen, Derk, Fabisch, Maria, Gausling, Lisa and Schnetz, Karin ORCID: 0000-0003-4693-6202 (2016). Interaction of the RcsB Response Regulator with Auxiliary Transcription Regulators in Escherichia coli. J. Biol. Chem., 291 (5). S. 2357 - 2371. BETHESDA: AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC. ISSN 1083-351X
Full text not available from this repository.Abstract
The Rcs phosphorelay is a two-component signal transduction system that is induced by cell envelope stress. RcsB, the response regulator of this signaling system, is a pleiotropic transcription regulator, which is involved in the control of various stress responses, cell division, motility, and biofilm formation. RcsB regulates transcription either as a homodimer or together with auxiliary regulators, such as RcsA, BglJ, and GadE in Escherichia coli. In this study, we show that RcsB in addition forms heterodimers with MatA (also known as EcpR) and with DctR. Our data suggest that the MatA-dependent transcription regulation is mediated by the MatA-RcsB heterodimer and is independent of RcsB phosphorylation. Furthermore, we analyzed the relevance of amino acid residues of the active quintet of conserved residues, and of surface-exposed residues for activity of RcsB. The data suggest that the activity of the phosphorylation-dependent dimers, such as RcsA-RcsB and RcsB-RcsB, is affected by mutation of residues in the vicinity of the phosphorylation site, suggesting that a phosphorylation-induced structural change modulates their activity. In contrast, the phosphorylation-independent heterodimers BglJ-RcsB and MatA-RcsB are affected by only very few mutations. Heterodimerization of RcsB with various auxiliary regulators and their differential dependence on phosphorylation add an additional level of control to the Rcs system that is operating at the output level.
Item Type: | Journal Article | ||||||||||||||||||||
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URN: | urn:nbn:de:hbz:38-286908 | ||||||||||||||||||||
DOI: | 10.1074/jbc.M115.696815 | ||||||||||||||||||||
Journal or Publication Title: | J. Biol. Chem. | ||||||||||||||||||||
Volume: | 291 | ||||||||||||||||||||
Number: | 5 | ||||||||||||||||||||
Page Range: | S. 2357 - 2371 | ||||||||||||||||||||
Date: | 2016 | ||||||||||||||||||||
Publisher: | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | ||||||||||||||||||||
Place of Publication: | BETHESDA | ||||||||||||||||||||
ISSN: | 1083-351X | ||||||||||||||||||||
Language: | English | ||||||||||||||||||||
Faculty: | Faculty of Mathematics and Natural Sciences | ||||||||||||||||||||
Divisions: | Faculty of Mathematics and Natural Sciences > Department of Biology > Institute for Genetics | ||||||||||||||||||||
Subjects: | no entry | ||||||||||||||||||||
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Refereed: | Yes | ||||||||||||||||||||
URI: | http://kups.ub.uni-koeln.de/id/eprint/28690 |
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