Rapid expansion of the protein disulfide isomerase gene family facilitates the folding of venom peptides.

ABSTRACT: Formation of correct disulfide bonds in the endoplasmic reticulum is a crucial step for folding proteins destined for secretion. Protein disulfide isomerases (PDIs) play a central role in this process. We report a previously unidentified, hypervariable family of PDIs that represents the most diverse gene family of oxidoreductases described in a single genus to date. These enzymes are highly expressed specifically in the venom glands of predatory cone snails, animals that synthesize a remarkably diverse set of cysteine-rich peptide toxins (conotoxins). Enzymes in this PDI family, termed conotoxin-specific PDIs, significantly and differentially accelerate the kinetics of disulfide-bond formation of several conotoxins. Our results are consistent with a unique biological scenario associated wi

SUBMITTER: Safavi-Hemami H 

PROVIDER: S-EPMC4812716 | biostudies-literature | 2016 Mar

REPOSITORIES: biostudies-literature