The CHAP domain of Cse functions as an endopeptidase that acts at mature septa to promoteStreptococcus thermophiluscell separation - Archive ouverte HAL
Article Dans Une Revue Molecular Microbiology Année : 2009

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

Joëlle Gérard
  • Fonction : Auteur
Valérie Legué
Marie-Pierre Chapot-Chartier
Pascal Courtin
  • Fonction : Auteur
Frédéric Borges
  • Fonction : Auteur
Bernard Decaris
  • Fonction : Auteur
Nathalie Leblond-Bourget
  • Fonction : Auteur

Résumé

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 subtilis 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.

Dates et versions

hal-03649054 , version 1 (22-04-2022)

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Citer

Séverine Layec, Joëlle Gérard, Valérie Legué, Marie-Pierre Chapot-Chartier, Pascal Courtin, et al.. The CHAP domain of Cse functions as an endopeptidase that acts at mature septa to promoteStreptococcus thermophiluscell separation. Molecular Microbiology, 2009, pp.1205 - 1217. ⟨10.1111/j.1365-2958.2009.06595.x⟩. ⟨hal-03649054⟩

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