Activity and regulation of various forms of CwlJ, SleB, and YpeB proteins in degrading cortex peptidoglycan of spores of Bacillus species in vitro and during spore germination.

ABSTRACT: Germination of Bacillus spores requires degradation of a modified layer of peptidoglycan (PG) termed the spore cortex by two redundant cortex-lytic enzymes (CLEs), CwlJ and SleB, plus SleB's partner protein, YpeB. In this study, in vitro and in vivo analyses have been used to clarify the roles of individual SleB and YpeB domains in PG degradation. Purified mature Bacillus cereus SleB without its signal sequence (SleB(M)) and the SleB C-terminal catalytic domain (SleB(C)) efficiently triggered germination of decoated Bacillus megaterium and Bacillus subtilis spores lacking endogenous CLEs; previously, SleB's N-terminal domain (SleB(N)) was shown to bind PG but have no enzymatic activity. YpeB lacking its putative membrane anchoring sequence (YpeB(M)) or its N- and C-terminal domains (YpeB(N

SUBMITTER: Li Y 

PROVIDER: S-EPMC3676066 | biostudies-literature | 2013 Jun

REPOSITORIES: biostudies-literature