Stable Signal Peptides and the Response to Secretion Stress in Staphylococcus aureus.

ABSTRACT: Protein secretion is essential, but how it is managed is poorly understood. In bacteria, most secreted proteins require release from the outer surface of the cytoplasmic membrane by type I signal peptidase (SPase), which cleaves the mature protein from its membrane-bound N-terminal signal peptide. As the first step that occurs outside the protected cytoplasmic environment and because insufficient activity can rapidly result in the toxic accumulation of preproteins, the activity of SPase is expected to be closely monitored and perhaps supplemented when insufficient. Indeed, we previously demonstrated that inhibition of SPase in Staphylococcus aureus results in derepression of the ayrRABC operon, which encodes an alternate mechanism to release proteins. However, in this case, t

SUBMITTER: Craney A 

PROVIDER: S-EPMC5727409 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature