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A common dimerization interface in bacterial response regulators KdpE and TorR

¹ Department of Chemistry and Chemical Biology, Rutgers University, Piscataway, New Jersey 08854, USA
² Center for Advanced Biotechnology and Medicine and ³ Howard Hughes Medical Institute, Piscataway, New Jersey 08854, USA
⁴ Department of Biochemistry, University of Medicine and Dentistry of New Jersey, Robert Wood Johnson Medical School, Piscataway, New Jersey 08854, USA

(RECEIVED July 23, 2005; FINAL REVISION September 1, 2005; ACCEPTED September 1, 2005)

Bacterial response regulators are key regulatory proteins that function as the final elements of so-called two-component signaling systems. The activities of response regulators in vivo are modulated by phosphorylation that results from interactions between the response regulator and its cognate histidine protein kinase. The level of response regulator phosphorylation, which is regulated by intra-or extracellular signals sensed by the histidine protein kinase, ultimately determines the output response that is initiated or carried out by the response regulator. We have recently hypothesized that in the OmpR/PhoB subfamily of response regulator transcription factors, this activation involves a common mechanism of dimerization using a set of highly conserved residues in the 4–5–5 face. Here we report the X-ray crystal structures of the regulatory domains of response regulators TorR (1.8 Å), Ca²⁺-bound KdpE (2.0 Å), and Mg²⁺/BeF₃^–-bound KdpE (2.2 Å), both members of the OmpR/ PhoB subfamily from Escherichia coli. Both regulatory domains form symmetric dimers in the asymmetric unit that involve the 4–5–5 face. As observed previously in other OmpR/PhoB response regulators, the dimer interfaces are mediated by highly conserved residues within this subfamily. These results provide further evidence that most all response regulators of the OmpR/ PhoB subfamily share a common mechanism of activation by dimerization.

Keywords: phosphorylation; transcription regulation; response regulator; TMAO respiratory system; Kdp K⁺ transport system

Abbreviations: TCS(s), two-component system(s) • RR(s), response regulator(s) • KdpE_N, KdpE regulatory domain • TorR_N, TorR regulatory domain • NCS, noncrystallographic symmetry • RMSD, root mean square deviation • TMAO, trimethylamine N-oxide • SeMet, seleno-methionine • ME, -mercaptoethanol • PDB, Protein Data Bank

Article and publication are at http://www.proteinscience.org/cgi/doi/10.1110/ps.051722805.

Reprint requests to: Ann M. Stock, Center for Advanced Biotechnology and Medicine, 679 Hoes Lane, Piscataway, NJ 08854, USA; e-mail: stock{at}cabm.rutgers.edu; fax: (732) 235-5289.

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