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

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Standard

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 Krogh; Bandyopadhyay, Pradip K.; Gruber, Christian W.; Purcell, Anthony W.; Yandell, Mark; Olivera, Baldomero M.; Ellgaard, Lars.

I: Proceedings of the National Academy of Sciences of the United States of America, Bind 113, Nr. 12, 2016, s. 3227-3232.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Safavi-Hemami, H, Li, Q, Jackson, RL, Song, AS, Boomsma, WK, Bandyopadhyay, PK, Gruber, CW, Purcell, AW, Yandell, M, Olivera, BM & Ellgaard, L 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, bind 113, nr. 12, s. 3227-3232. https://doi.org/10.1073/pnas.1525790113

APA

Safavi-Hemami, H., Li, Q., Jackson, R. L., Song, A. S., Boomsma, W. K., Bandyopadhyay, P. K., Gruber, C. W., Purcell, A. W., Yandell, M., Olivera, B. M., & Ellgaard, L. (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. https://doi.org/10.1073/pnas.1525790113

Vancouver

Safavi-Hemami H, Li Q, Jackson RL, Song AS, Boomsma WK, Bandyopadhyay PK o.a. 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. 2016;113(12):3227-3232. https://doi.org/10.1073/pnas.1525790113

Author

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

Bibtex

@article{509991fecca44f44a6c121e3caf75dc4,
title = "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 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.",
author = "Helena Safavi-Hemami and Qing Li and Jackson, {Ronneshia L.} and Song, {Albert S.} and Boomsma, {Wouter Krogh} and Bandyopadhyay, {Pradip K.} and Gruber, {Christian W.} and Purcell, {Anthony W.} and Mark Yandell and Olivera, {Baldomero M.} and Lars Ellgaard",
year = "2016",
doi = "10.1073/pnas.1525790113",
language = "English",
volume = "113",
pages = "3227--3232",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
publisher = "The National Academy of Sciences of the United States of America",
number = "12",

}

RIS

TY - JOUR

T1 - Rapid expansion of the protein disulfide isomerase gene family facilitates the folding of venom peptides

AU - Safavi-Hemami, Helena

AU - Li, Qing

AU - Jackson, Ronneshia L.

AU - Song, Albert S.

AU - Boomsma, Wouter Krogh

AU - Bandyopadhyay, Pradip K.

AU - Gruber, Christian W.

AU - Purcell, Anthony W.

AU - Yandell, Mark

AU - Olivera, Baldomero M.

AU - Ellgaard, Lars

PY - 2016

Y1 - 2016

N2 - 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.

AB - 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.

U2 - 10.1073/pnas.1525790113

DO - 10.1073/pnas.1525790113

M3 - Journal article

C2 - 26957604

VL - 113

SP - 3227

EP - 3232

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 12

ER -

ID: 160125168