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Originally published In Press as doi:10.1074/jbc.M412741200 on November 29, 2004

J. Biol. Chem., Vol. 280, Issue 6, 4089-4094, February 11, 2005
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Signal-dependent Binding of the Response Regulators PhoP and PmrA to Their Target Promoters in Vivo*

Dongwoo Shin and Eduardo A. Groisman{ddagger}

From the Department of Molecular Microbiology, Howard Hughes Medical Institute, Washington University School of Medicine, St. Louis, Missouri 63110

Low Mg2+ promotes phosphorylation of the response regulators PhoP and PmrA and transcription of their activated genes in Salmonella enterica. Using chromatin immunoprecipitation, we have now determined that the PhoP and PmrA proteins are recruited to the regulatory region of their target genes when bacteria experience low Mg2+ but not when they are grown in high Mg2+. Even when the PhoP protein was artificially produced at 4-fold higher levels than the wild-type strain, promoter occupancy required the low Mg2+ signal. Substitution of the predicted phosphorylation site Asp-52 with a valine residue abolished phosphorylation of the PhoP protein, resulting in loss of PhoP binding to target promoters and transcription of PhoP-activated genes. Our results indicate that the promoter binding ability of the PhoP and PmrA proteins occurring in low Mg2+ is correlated with phosphorylation of these proteins in vivo.

Received for publication, November 10, 2004 , and in revised form, November 24, 2004.

* This work was supported in part by National Institutes of Health Grant AI49561 (to E. A. G.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

{ddagger} Investigator of the Howard Hughes Medical Institute. To whom correspondence should be addressed. Tel.: 314-362-3692; Fax: 314-747-8228; E-mail: groisman{at}borcim.wustl.edu.


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