The peroxisomal AAA-ATPase Pex1/Pex6 unfolds substrates by processive threading

Brooke M. Gardner; Dominic T. Castanzo; Saikat Chowdhury; Goran Stjepanovic; Matthew S. Stefely; James H. Hurley; Gabriel C. Lander; Andreas Martin

doi:10.1038/s41467-017-02474-4

Nature Communications (Jan 2018)

The peroxisomal AAA-ATPase Pex1/Pex6 unfolds substrates by processive threading

Brooke M. Gardner,
Dominic T. Castanzo,
Saikat Chowdhury,
Goran Stjepanovic,
Matthew S. Stefely,
James H. Hurley,
Gabriel C. Lander,
Andreas Martin

Affiliations

Brooke M. Gardner: Department of Molecular and Cell Biology, University of California, Berkeley
Dominic T. Castanzo: Department of Molecular and Cell Biology, University of California, Berkeley
Saikat Chowdhury: Department of Integrative Structural and Computational Biology, The Scripps Research Institute
Goran Stjepanovic: Department of Molecular and Cell Biology, University of California, Berkeley
Matthew S. Stefely: Department of Molecular and Cell Biology, University of California, Berkeley
James H. Hurley: Department of Molecular and Cell Biology, University of California, Berkeley
Gabriel C. Lander: Department of Integrative Structural and Computational Biology, The Scripps Research Institute
Andreas Martin: Department of Molecular and Cell Biology, University of California, Berkeley

DOI: https://doi.org/10.1038/s41467-017-02474-4
Journal volume & issue: Vol. 9, no. 1
pp. 1 – 15

Abstract

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Pex1 and Pex6 form a heterohexameric Type-2 AAA-ATPase motor whose function in peroxisomal matrix-protein import is still debated. Here, the authors combine structural, biochemical, and cell-biological approaches to show that Pex1/Pex6 is a protein unfoldase, which supports a role in mechanical unfolding of peroxin proteins.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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