Title |
Rapid expansion of the protein disulfide isomerase gene family facilitates the folding of venom peptides
|
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Published in |
Proceedings of the National Academy of Sciences of the United States of America, March 2016
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DOI | 10.1073/pnas.1525790113 |
Pubmed ID | |
Authors |
Helena Safavi-Hemami, Qing Li, Ronneshia L Jackson, Albert S Song, Wouter Boomsma, Pradip K Bandyopadhyay, Christian W Gruber, Anthony W Purcell, Mark Yandell, Baldomero M Olivera, Lars Ellgaard |
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 with protein folding: The diversification of a family of foldases can be correlated with the rapid evolution of an unprecedented diversity of disulfide-rich structural domains expressed by venomous marine snails in the superfamily Conoidea. |
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