An asymmetric heterodomain interface stabilizes a response regulator–DNA complex

Anoop Narayanan, Shivesh Kumar, Amanda N. Evrard, Lake N. Paul and Dinesh A. Yernool ()
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Anoop Narayanan: Purdue University
Shivesh Kumar: Purdue University
Amanda N. Evrard: Purdue University
Lake N. Paul: Bindley Bioscience Center, Purdue University
Dinesh A. Yernool: Purdue University

Nature Communications, 2014, vol. 5, issue 1, 1-9

Abstract: Abstract Two-component signal transduction systems consist of pairs of histidine kinases and response regulators, which mediate adaptive responses to environmental cues. Most activated response regulators regulate transcription by binding tightly to promoter DNA via a phosphorylation-triggered inactive-to-active transition. The molecular basis for formation of stable response regulator–DNA complexes that precede the assembly of RNA polymerases is unclear. Here, we present structures of DNA complexed with the response regulator KdpE, a member of the OmpR/PhoB family. The distinctively asymmetric complex in an active-like conformation reveals a unique intramolecular interface between the receiver domain (RD) and the DNA-binding domain (DBD) of only one of the two response regulators in the complex. Structure–function studies show that this RD–DBD interface is necessary to form stable complexes that support gene expression. The conservation of sequence and structure suggests that these findings extend to a large group of response regulators that act as transcription factors.

Date: 2014
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DOI: 10.1038/ncomms4282

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