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

Safavi-Hemami, Helena, Li, Qing, Jackson, Ronneshia L., Song, Albert S., Boomsma, Wouter, Bandyopadhyay, Pradip K., Gruber, Christian W., Purcell, Anthony W., Yandell, Mark, Olivera, Baldomero M. and Ellgaard, Lars (2016) Rapid expansion of the protein disulfide isomerase gene family facilitates the folding of venom peptides. Proceedings of the National Academy of Sciences of the United States of America, 113 12: 3227-3232. doi:10.1073/pnas.1525790113


Author Safavi-Hemami, Helena
Li, Qing
Jackson, Ronneshia L.
Song, Albert S.
Boomsma, Wouter
Bandyopadhyay, Pradip K.
Gruber, Christian W.
Purcell, Anthony W.
Yandell, Mark
Olivera, Baldomero M.
Ellgaard, Lars
Title Rapid expansion of the protein disulfide isomerase gene family facilitates the folding of venom peptides
Journal name Proceedings of the National Academy of Sciences of the United States of America   Check publisher's open access policy
ISSN 0027-8424
1091-6490
Publication date 2016-03-22
Year available 2016
Sub-type Article (original research)
DOI 10.1073/pnas.1525790113
Open Access Status Not Open Access
Volume 113
Issue 12
Start page 3227
End page 3232
Total pages 6
Place of publication Washington, DC, United States
Publisher National Academy of Sciences
Collection year 2017
Language eng
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 conotoxinspecific 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 disulfiderich structural domains expressed by venomous marine snails in the superfamily Conoidea.
Keyword Protein disulfide isomerase
Peptide folding
Gene expansion
Cone snail venom
Conotoxins
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: HERDC Pre-Audit
School of Biomedical Sciences Publications
 
Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 0 times in Thomson Reuters Web of Science Article
Scopus Citation Count Cited 0 times in Scopus Article
Google Scholar Search Google Scholar
Created: Sun, 17 Apr 2016, 00:22:59 EST by System User on behalf of Learning and Research Services (UQ Library)