Autoproteolytic mechanism of CdiA toxin release reconstituted <i>in vitro</i>.

ABSTRACT: Contact-dependent inhibition (CDI) is a mechanism of interbacterial competition in Gram-negative bacteria. Bacteria that contain CDI systems produce a large, filamentous protein, CdiA, on their cell surfaces. CdiA contains a C-terminal toxin domain that is transported across the outer membranes (OMs) of neighboring bacteria. Once inside a target bacterium, the toxin is released from the CdiA protein via a proteolytic mechanism that has not been well characterized. We have developed an in vitro assay to monitor this toxin release process and have identified several conserved amino acids that play critical roles in the autocatalytic mechanism. Our results indicate that a hydrophobic, membrane-like environment is required for CdiA to fold, and the proteolysis occurs through an asparagi

SUBMITTER: Tiu AKY 

PROVIDER: S-EPMC11500576 | biostudies-literature | 2024 Oct

REPOSITORIES: biostudies-literature