Rapid expansion of the protein disulfide isomerase gene family facilitates the folding of venom peptides
Research output: Contribution to journal › Journal article › Research › peer-review
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.
Original language | English |
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Journal | Proceedings of the National Academy of Sciences of the United States of America |
Volume | 113 |
Issue number | 12 |
Pages (from-to) | 3227-3232 |
Number of pages | 6 |
ISSN | 0027-8424 |
DOIs | |
Publication status | Published - 2016 |
ID: 160125168