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J. Biol. Chem., Vol. 280, Issue 17, 16695-16704, April 29, 2005

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Identification of the Putative Staphylococcal AgrB Catalytic Residues Involving the Proteolytic Cleavage of AgrD to Generate Autoinducing Peptide^*

Rongde Qiu, Wuhong Pei, Linsheng Zhang¶, Jianqun Lin, and Guangyong Ji||**

From the Department of Microbiology and Immunology, Uniformed Services University of the Health Sciences, Bethesda, Maryland 20814 and the ^||Department of Biology, The Catholic University of America, Washington, D. C. 20064

The P2 operon of the staphylococcal accessory gene regulator (agr) encodes four genes (agrA, -B, -C, and -D) whose products compose a quorum sensing system: AgrA and AgrC resemble a two-component signal transduction system of which AgrC is a sensor kinase and AgrA is a response regulator; AgrD, a polypeptide that is integrated into the cytoplasmic membrane via an amphipathic -helical motif in its N-terminal region, is the propeptide for an autoinducing peptide that is the ligand for AgrC; and AgrB is a novel membrane protein that involves in the processing of AgrD propeptide and possibly the secretion of the mature autoinducing peptide. In this study, we demonstrated that AgrB had endopeptidase activity, and identified 2 amino acid residues in AgrB (cysteine 84 and histidine 77) that might form a putative cysteine endopeptidase catalytic center in the proteolytic cleavage of AgrD at its C-terminal processing site. Computer analysis revealed that the cysteine and histidine residues were conserved among the potential AgrB homologous proteins, suggesting that the Agr quorum sensing system homologues might also exist in other Gram-positive bacteria.

Received for publication, October 5, 2004 , and in revised form, February 24, 2005.

^* This work was supported by National Institutes of Health Grant R01AI46445 (to G. J.). 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.

Both authors contributed equally to this study.

^¶ Present address: Division of Pediatric Oncology, The Johns Hopkins University, 1650 Orleans St., Baltimore, MD 21231.

^** To whom correspondence should be addressed: Dept. of Biology, The Catholic University of America, 620 Michigan Ave. NE, Washington, D.C. 20064. Tel.: 202-319-5278; Fax: 202-319-5721; E-mail: ji{at}cua.edu.

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