The CHAP domain of Cse functions as an endopeptidase that acts at mature septa to promoteStreptococcus thermophiluscell separation

Autor: Joëlle Gérard, Séverine Layec, Nathalie Leblond-Bourget, Valérie Legué, Marie-Pierre Chapot-Chartier, Bernard Decaris, Frédéric Borges, Pascal Courtin
Přispěvatelé: Laboratoire de génétique et microbiologie (LGM), Institut National de la Recherche Agronomique (INRA)-Université Henri Poincaré - Nancy 1 (UHP), Interactions Arbres-Microorganismes (IAM), Université de Lorraine (UL)-Institut National de la Recherche Agronomique (INRA), Biochimie bactérienne (BIOBAC), Institut National de la Recherche Agronomique (INRA), Institut National de la Recherche Agronomique (INRA)-Université de Lorraine (UL), Ministere de l'Education Nationale de l'Enseignement Superieur et de la Recherche
Rok vydání: 2009
Předmět:
Streptococcus thermophilus
Genetic and Microbiology Gérard
Cell division
ecophysiology and functional ecology Legué
Bacillus subtilis
Nancy University
chemistry.chemical_compound
Cell Wall
mature septa
ecophysiology and functional ecology Chapot-Chartier
Frédéric
MESH: Endopeptidases
MESH: Bacterial Proteins
ENSAIA
MESH: Genetic Complementation Test
0303 health sciences
biology
Bacterial Biochemistry Borges
Immunogold labelling
Bernard
Genetic and Microbiology Key Words: peptidoglycan hydrolase
[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry
Molecular Biology/Biomolecules [q-bio.BM]
RNA
Bacterial
Pascal
Biochemistry
MESH: Cell Division
LSGA Decaris
MESH: RNA
Bacterial
Cell Division
MESH: Mutation
Séverine
CHAP domain
Bacterial Biochemistry Courtin
Complete List of Authors: Layec
Microbiology
Valérie
MESH: Streptococcus thermophilus
Cell wall
03 medical and health sciences
MESH: Cell Wall
Bacterial Proteins
Endopeptidases
parasitic diseases
Hydrolase
Protein Interaction Domains and Motifs
Molecular Biology
030304 developmental biology
MESH: Protein Interaction Domains and Motifs
030306 microbiology
Genetic Complementation Test
Joelle
INRA
[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry
Molecular Biology/Molecular biology
biology.organism_classification
Marie-Pierre
[SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology
Genetic and Microbiology Leblond-Bourget
chemistry
Nathalie
Mutation
cell separation
Genomic
Peptidoglycan
Zdroj: Molecular Microbiology
Molecular Microbiology, Wiley, 2009, 71 (5), pp.1205-1217. ⟨10.1111/j.1365-2958.2009.06595.x⟩
ISSN: 1365-2958
0950-382X
DOI: 10.1111/j.1365-2958.2009.06595.x
Popis: International audience; Cell separation is dependent on cell wall hydrolases that cleave the peptidoglycan shared between daughter cells. In Streptococcus thermophilus, this step is performed by the Cse protein whose depletion resulted in the formation of extremely long chains of cells. Cse, a natural chimeric enzyme created by domain shuffling, carries at least two important domains for its activity: the LysM expected to be responsible for the cell wall-binding and the CHAP domain predicted to contain the active centre. Accordingly, the localization of Cse on S. thermophilus cell surface has been undertaken by immunogold electron and immunofluorescence microscopies using of antibodies raised against the N-terminal end of this protein. Immunolocalization shows the presence of the Cse protein at mature septa. Moreover, the CHAP domain of Cse exhibits a cell wall lytic activity in zymograms performed with cell walls of Micrococcus lysodeikticus, Bacillus sub-tilis and S. thermophilus. Additionally, RP-HPLC analysis of muropeptides released from B. subtilis and S. thermophilus cell wall after digestion with the CHAP domain shows that Cse is an endopeptidase. Altogether, these results suggest that Cse is a cell wall hydrolase involved in daughter cell separation of S. thermophilus.
Databáze: OpenAIRE
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