Interaction of intramembrane metalloprotease SpoIVFB with substrate Pro-σ^K.

ABSTRACT: Intramembrane proteases (IPs) cleave membrane-associated substrates in nearly all organisms and regulate diverse processes. A better understanding of how these enzymes interact with their substrates is necessary for rational design of IP modulators. We show that interaction of Bacillus subtilis IP SpoIVFB with its substrate Pro-σ^K depends on particular residues in the interdomain linker of SpoIVFB. The linker plus either the N-terminal membrane domain or the C-terminal cystathione-β-synthase (CBS) domain of SpoIVFB was sufficient for the interaction but not for cleavage of Pro-σ^K Chemical cross-linking and mass spectrometry of purified, inactive SpoIVFB-Pro-σ^K complex indicated residues of the two proteins in proximity. A structural model of the comp

SUBMITTER: Halder S 

PROVIDER: S-EPMC5740621 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature