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J Mol Biol. 2015 Mar 27;427(6 Pt B):1375-88. doi: 10.1016/j.jmb.2015.01.019. Epub 2015 Feb 7.

The Pex1/Pex6 complex is a heterohexameric AAA+ motor with alternating and highly coordinated subunits.

Author information

1
Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720-3200, USA; Miller Institute for Basic Research in Science, University of California, Berkeley, Berkeley, CA 94720, USA.
2
Department of Integrative Structural and Computational Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
3
Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720-3200, USA; California Institute for Quantitative Biosciences, University of California, Berkeley, Berkeley, CA 94720-3220, USA. Electronic address: a.martin@berkeley.edu.

Abstract

Pex1 and Pex6 are Type-2 AAA+ ATPases required for the de novo biogenesis of peroxisomes. Mutations in Pex1 and Pex6 account for the majority of the most severe forms of peroxisome biogenesis disorders in humans. Here, we show that the ATP-dependent complex of Pex1 and Pex6 from Saccharomyces cerevisiae is a heterohexamer with alternating subunits. Within the Pex1/Pex6 complex, only the D2 ATPase ring hydrolyzes ATP, while nucleotide binding in the D1 ring promotes complex assembly. ATP hydrolysis by Pex1 is highly coordinated with that of Pex6. Furthermore, Pex15, the membrane anchor required for Pex1/Pex6 recruitment to peroxisomes, inhibits the ATP-hydrolysis activity of Pex1/Pex6.

KEYWORDS:

AAA+ ATPase; Pex1; Pex15; Pex6; peroxisome

PMID:
25659908
PMCID:
PMC4355278
DOI:
10.1016/j.jmb.2015.01.019
[Indexed for MEDLINE]
Free PMC Article
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