期刊
NATURE COMMUNICATIONS
卷 9, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/s41467-017-02474-4
关键词
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资金
- U.C. Office of the President, Multicampus Research Programs and Initiatives grant [MR-15-328599]
- Program for Breakthrough Biomedical Research - Sandler Foundation
- Office of Science, Office of Basic Energy Sciences, of the U.S. Department of Energy [DE-AC02-05CH11231]
- NIH [S10 OD016268]
- Miller Institute for Basic Research in Science, University of California, Berkeley
- National Institute Of General Medical Sciences [K99GM121880]
- Howard Hughes Medical Institute
- US National Institutes of Health [R01-GM094497]
- US National Science Foundation CAREER Program [NSF-MCB-1150288]
- Pew Scholars program
- Searle Scholars program
- NIH grant [DP2 EB020402-01]
Pex1 and Pex6 form a heterohexameric motor essential for peroxisome biogenesis and function, and mutations in these AAA-ATPases cause most peroxisome-biogenesis disorders in humans. The tail-anchored protein Pex15 recruits Pex1/Pex6 to the peroxisomal membrane, where it performs an unknown function required for matrix-protein import. Here we determine that Pex1/Pex6 from S. cerevisiae is a protein translocase that unfolds Pex15 in a pore-loop-dependent and ATP-hydrolysis-dependent manner. Our structural studies of Pex15 in isolation and in complex with Pex1/Pex6 illustrate that Pex15 binds the N-terminal domains of Pex6, before its C-terminal disordered region engages with the pore loops of the motor, which then processively threads Pex15 through the central pore. Furthermore, Pex15 directly binds the cargo receptor Pex5, linking Pex1/Pex6 to other components of the peroxisomal import machinery. Our results thus support a role of Pex1/Pex6 in mechanical unfolding of peroxins or their extraction from the peroxisomal membrane during matrix-protein import.
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