Format

Send to

Choose Destination
J Biol Chem. 2016 Jan 29;291(5):2357-70. doi: 10.1074/jbc.M115.696815. Epub 2015 Dec 3.

Interaction of the RcsB Response Regulator with Auxiliary Transcription Regulators in Escherichia coli.

Author information

1
From the Institute for Genetics, University of Cologne, Zülpicher Strasse 47a, 50674 Cologne, Germany.
2
From the Institute for Genetics, University of Cologne, Zülpicher Strasse 47a, 50674 Cologne, Germany schnetz@uni-koeln.de.

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.

KEYWORDS:

DNA binding protein; bacterial signal transduction; protein phosphorylation; protein-protein interaction; transcription coregulator

PMID:
26635367
PMCID:
PMC4732218
DOI:
10.1074/jbc.M115.696815
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for HighWire Icon for PubMed Central
Loading ...
Support Center