Screening a library of temperature-sensitive mutants to identify secretion factors in <i>Staphylococcus aureus</i>.
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ABSTRACT: Protein secretion is an essential cell process in bacteria, required for cell envelope biogenesis, export of virulence factors, and acquisition of nutrients, among other important functions. In the Sec secretion pathway, signal peptide-bearing precursors are recognized by the SecA ATPase and pushed across the membrane through a translocon channel made of the proteins SecY, SecE, and SecG. The Sec pathway has been extensively studied in the model organism Escherichia coli, but the Sec pathways of other bacteria such as the human pathogen Staphylococcus aureus differ in important ways from this model. Unlike in E. coli, a subset of precursors in S. aureus contains a YSIRK/GXXS (YSIRK) motif in an extended signal peptide. These proteins are secreted into the cross-
SUBMITTER: Leddy O
PROVIDER: S-EPMC11841065 | biostudies-literature | 2025 Feb
REPOSITORIES: biostudies-literature
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