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Papers In Press, published online ahead of print February 25, 2005
J. Biol. Chem, 10.1074/jbc.M411372200
Submitted on October 5, 2004
Revised on February 24, 2005
Accepted on February 25, 2005

Identification of the putative staphylococcal AgrB catalytic residues involving in the proteolytic cleavage of AgrD to generate autoinducing peptide

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

Department of Biology, Catholic University of America, Washington, DC 20064

Corresponding Author: ji{at}cua.edu

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 a-helical motif in its N-terminal region, is the propeptide for an autoinducing peptide (AIP) 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 AIP. In this study, we demonstrated that AgrB had endopeptidase activity, and identified two amino acid residues in AgrB (Cysteine 84 and Histine 77) that might form a putative cysteine endopeptidase catalytic center involving 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 Agr quorum sensing system homologues might also exist in other Gram-positive bacteria.


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