Article
The CHAP domain of Cse functions as an endopeptidase that acts at mature septa to promote Streptococcus thermophilus cell separation.
Molecular microbiology - 1 Mar 2009
Layec Séverine, Gérard Joëlle, Legué Valérie, Chapot-Chartier Marie-Pierre, Courtin Pascal, Borges Frédéric, Decaris Bernard, Leblond-Bourget Nathalie
Abstract excerpt
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...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.