Identification of residues important for cleavage of the extracellular signaling peptide CSF of Bacillus subtilis from its precursor protein.

ABSTRACT: Extracellular Phr pentapeptides produced by gram-positive, spore-forming bacteria regulate processes during the transition from exponential- to stationary-phase growth. Phr pentapeptides are produced by cleavage of their precursor proteins. We determined the residues that direct this cleavage for the Bacillus subtilis Phr peptide, CSF, which is derived from the C terminus of PhrC. Strains expressing PhrC with substitutions in residues -1 to -5 relative to the cleavage site had a defect in CSF production. The mutant PhrC proteins retained a functional signal sequence for secretion, as assessed by secretion of PhrC-PhoA fusions. To determine whether the substitutions directly affected cleavage of PhrC to CSF, we tested cleavage of synthetic pro-CSF peptides that corresponded to the C terminu

SUBMITTER: Lanigan-Gerdes S 

PROVIDER: S-EPMC2566178 | biostudies-literature | 2008 Oct

REPOSITORIES: biostudies-literature