National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
R01-GM094497
United States
National Science Foundation (NSF, United States)
NSF-MCB-1150288
United States
Citation
Journal: Nat Commun / Year: 2018 Title: The peroxisomal AAA-ATPase Pex1/Pex6 unfolds substrates by processive threading. Authors: Brooke M Gardner / Dominic T Castanzo / Saikat Chowdhury / Goran Stjepanovic / Matthew S Stefely / James H Hurley / Gabriel C Lander / Andreas Martin / Abstract: 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 ...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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