SpxB Regulates O-Acetylation-dependent Resistance of Lactococcus lactis Peptidoglycan to Hydrolysis
| Autor: | Michael Erkelenz, Girbe Buist, Oscar P. Kuipers, Aurélie Maisons, Dorte Frees, Peggy Mervelet, Philippe Noirot, Alexandra Gruss, Jan Kok, Sylviane Furlan, Patrick Veiga, Carmen Bulbarela-Sampieri, Saulius Kulakauskas, Marie-Pierre Chapot-Chartier |
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| Přispěvatelé: | Groningen Biomolecular Sciences and Biotechnology, Molecular Genetics |
| Rok vydání: | 2007 |
| Předmět: |
GRAM-POSITIVE BACTERIA
STREPTOCOCCUS-PNEUMONIAE 2-COMPONENT SYSTEM Peptidoglycan Bacillus subtilis Biochemistry Bacterial cell structure BACILLUS-SUBTILIS Cell wall chemistry.chemical_compound Bacterial Proteins N-ACETYLGLUCOSAMINIDASE Acetyltransferases Cell Wall RNA polymerase CELL-WALL COMPLETE GENOME SEQUENCE Animals Molecular Biology STAPHYLOCOCCUS-AUREUS biology Hydrolysis Lactococcus lactis Acetylation DNA-Directed RNA Polymerases N-Acetylmuramoyl-L-alanine Amidase Cell Biology SUBSP CREMORIS MG1363 biology.organism_classification chemistry Acetylesterase Genes Lethal Muramidase Lysozyme Cell envelope LYSOZYME-RESISTANCE Transcription Factors |
| Zdroj: | The Journal of Biological Chemistry, 282(27), 19342-19354. AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.m611308200 |
| Popis: | 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 PGO-acetylation by this cascade renders it resistant to hydrolysis. |
| Databáze: | OpenAIRE |
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