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Journal of Bacteriology, January 2002, p. 610-613, Vol. 184, No. 2
0021-9193/01/$04.00+0 DOI: 10.1128/JB.184.2.610-613.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.
Laboratoire de Microbiologie et Génétique Moléculaire, UMR 5100 CNRS-Université Paul Sabatier, 31062 Toulouse Cedex, France,1 Hoffmann-La Roche Ltd., CH-4070 Basel, Switzerland2
Received 16 August 2001/ Accepted 26 October 2001
Competence for genetic transformation of Streptococcus pneumoniae is a transient physiological property inducible by a competence-stimulating peptide (CSP). A 68-kDa CSP-inactivating protein was previously obtained following lithium chloride (LiCl) extraction. By the same protocol, a CSP-inactivating protein was purified and identified by matrix-assisted laser desorption ionization-time of flight mass spectrometry as an endopeptidase, PepO. Analysis of a pepO mutant provided no support for the hypothesis that PepO participates in competence regulation. To reconcile in vitro and in vivo data, we suggest that LiCl treatment results in the release of intracellular molecules, including PepO.
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