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SepM, a Streptococcal Protease Involved in Quorum Sensing, Displays Strict Substrate Specificity.


ABSTRACT:

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Streptococcus mutans, a causative agent of dental caries, relies on multiple quorum-sensing (QS) pathways that coordinate the expression of factors needed for colonization in the oral cavity. S. mutans uses small peptides as QS signaling molecules that typically are secreted into the outside milieu. Competence-stimulating peptide (CSP) is one such QS signaling molecule that functions through the ComDE two-component signal transduction pathway. CSP is secreted through NlmTE, a dedicated ABC transporter that cleaves off the N-terminal leader peptide to generate a mature peptide that is 21 residues long (CSP-21). We recently identified a surface-localized protease, SepM, which further cleaves the CSP-21 peptide at the C-terminal end and removes the last 3 residues to genera

SUBMITTER: Biswas S 

PROVIDER: S-EPMC4719462 | biostudies-literature | 2016 Feb

REPOSITORIES: biostudies-literature