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J. Biol. Chem., Vol. 282, Issue 27, 19342-19354, July 6, 2007

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SpxB Regulates O-Acetylation-dependent Resistance of Lactococcus lactis Peptidoglycan to Hydrolysis^*

Patrick Veiga¹², Carmen Bulbarela-Sampieri¹³, Sylviane Furlan, Aurélie Maisons, Marie-Pierre Chapot-Chartier, Michael Erkelenz⁴, Peggy Mervelet^¶, Philippe Noirot^¶, Dorte Frees^||, Oscar P. Kuipers^**, Jan Kok^**, Alexandra Gruss, Girbe Buist^**5, and Saulius Kulakauskas⁶

From the Unité Bactéries Lactiques et Pathogènes Opportunistes, Unité de Biochimie Bactérienne, and ^¶Génétique Microbienne, Institut National de la Recherche Agronomique, 78352 Jouy-en-Josas Cedex, France, the ^||Department of Veterinary Pathobiology, Royal Veterinary and Agricultural University, Stigbøjlen 4, DK-1870 Frederiksberg C, Denmark, and the ^**Department of Molecular Genetics, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands

Endogenous peptidoglycan (PG)-hydrolyzing enzymes, the autolysins, are needed to relax the rigid PG sacculus to allow bacterial cell growth and separation. PGs of pathogens and commensal bacteria may also be degraded by hydrolases of animal origin (lysozymes), which act as antimicrobials. The genetic mechanisms regulating PG resistance to hydrolytic degradation were dissected in the Gram-positive bacterium Lactococcus lactis. We found that the ability of L. lactis to counteract PG hydrolysis depends on the degree of acetylation. Overexpression of PG O-acetylase (encoded by oatA) led to bacterial growth arrest, indicating the potential lethality of oatA and a need for its tight regulation. A novel regulatory factor, SpxB (previously denoted as YneH), exerted a positive effect on oatA expression. Our results indicate that SpxB binding to RNA polymerase constitutes a previously missing link in the multistep response to cell envelope stress, provoked by PG hydrolysis with lysozyme. We suggest that the two-component system CesSR responds to this stress by inducing SpxB, thus favoring its interactions with RNA polymerase. Induction of PG O-acetylation by this cascade renders it resistant to hydrolysis.

Received for publication, December 11, 2006 , and in revised form, March 30, 2007.

^* This work was supported in part by an Aarden Levenswetenschappen middelgrote apparatuur grant for a transcriptomics facility from the Nederlandse Organisatie voor Wetenschappelijk Onderzoek (to O. P. K.). 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.

¹ Both authors contributed equally to this work.

² Supported by a thesis grant from the Region Ile de France and Institut National de la Recherche Agronomique and by European Molecular Biology Organization Fellowship ASTF 116-05.

³ Supported by Thesis Grant 68184 from the Consejo Nacional de Ciencia y Tecnologia.

⁴ Recipient of a fellowship from LabHealth under Marie Curie Contract MEST-CT-2004-514428.

⁵ Supported by Innovatiegerichte Onderzoeksprogramma Genomics Grant IGE01018. Present address: Dept. of Medical Microbiology, University Medical Center Groningen, University of Groningen, 9700 RB Groningen, The Netherlands.

⁶ To whom correspondence should be addressed. Tel.: 33-1-3465-2073; Fax: 33-1-3465-2065; E-mail: saulius.kulakauskas{at}jouy.inra.fr.

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