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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Nature Portfolio
2018-01-01
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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. |
first_indexed | 2024-12-19T03:50:33Z |
format | Article |
id | doaj.art-4061a2c4972642c8b618677d741846cd |
institution | Directory Open Access Journal |
issn | 2041-1723 |
language | English |
last_indexed | 2024-12-19T03:50:33Z |
publishDate | 2018-01-01 |
publisher | Nature Portfolio |
record_format | Article |
series | Nature Communications |
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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