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

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 unfo...

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Main Authors: Brooke M. Gardner, Dominic T. Castanzo, Saikat Chowdhury, Goran Stjepanovic, Matthew S. Stefely, James H. Hurley, Gabriel C. Lander, Andreas Martin
Format: Article
Language:English
Published: Nature Portfolio 2018-01-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-017-02474-4
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author Brooke M. Gardner
Dominic T. Castanzo
Saikat Chowdhury
Goran Stjepanovic
Matthew S. Stefely
James H. Hurley
Gabriel C. Lander
Andreas Martin
author_facet Brooke M. Gardner
Dominic T. Castanzo
Saikat Chowdhury
Goran Stjepanovic
Matthew S. Stefely
James H. Hurley
Gabriel C. Lander
Andreas Martin
author_sort Brooke M. Gardner
collection DOAJ
description 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.
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spelling doaj.art-4061a2c4972642c8b618677d741846cd2022-12-21T20:37:01ZengNature PortfolioNature Communications2041-17232018-01-019111510.1038/s41467-017-02474-4The peroxisomal AAA-ATPase Pex1/Pex6 unfolds substrates by processive threadingBrooke M. Gardner0Dominic T. Castanzo1Saikat Chowdhury2Goran Stjepanovic3Matthew S. Stefely4James H. Hurley5Gabriel C. Lander6Andreas Martin7Department of Molecular and Cell Biology, University of California, BerkeleyDepartment of Molecular and Cell Biology, University of California, BerkeleyDepartment of Integrative Structural and Computational Biology, The Scripps Research InstituteDepartment of Molecular and Cell Biology, University of California, BerkeleyDepartment of Molecular and Cell Biology, University of California, BerkeleyDepartment of Molecular and Cell Biology, University of California, BerkeleyDepartment of Integrative Structural and Computational Biology, The Scripps Research InstituteDepartment of Molecular and Cell Biology, University of California, BerkeleyPex1 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.https://doi.org/10.1038/s41467-017-02474-4
spellingShingle Brooke M. Gardner
Dominic T. Castanzo
Saikat Chowdhury
Goran Stjepanovic
Matthew S. Stefely
James H. Hurley
Gabriel C. Lander
Andreas Martin
The peroxisomal AAA-ATPase Pex1/Pex6 unfolds substrates by processive threading
Nature Communications
title The peroxisomal AAA-ATPase Pex1/Pex6 unfolds substrates by processive threading
title_full The peroxisomal AAA-ATPase Pex1/Pex6 unfolds substrates by processive threading
title_fullStr The peroxisomal AAA-ATPase Pex1/Pex6 unfolds substrates by processive threading
title_full_unstemmed The peroxisomal AAA-ATPase Pex1/Pex6 unfolds substrates by processive threading
title_short The peroxisomal AAA-ATPase Pex1/Pex6 unfolds substrates by processive threading
title_sort peroxisomal aaa atpase pex1 pex6 unfolds substrates by processive threading
url https://doi.org/10.1038/s41467-017-02474-4
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