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TitleThe peroxisomal AAA-ATPase Pex1/Pex6 unfolds substrates by processive threading.
Journal, issue, pagesNat Commun, Vol. 9, Issue 1, Page 135, Year 2018
Publish dateJan 10, 2018
AuthorsBrooke M Gardner / Dominic T Castanzo / Saikat Chowdhury / Goran Stjepanovic / Matthew S Stefely / James H Hurley / Gabriel C Lander / Andreas Martin /
PubMed AbstractPex1 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.
External linksNat Commun / PubMed:29321502 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.55 - 23.2 Å
Structure data

EMDB-7005:
Negative stain reconstruction of the peroxisomal AAA-ATPase Pex1/Pex6 complex associated with substrate Pex15
Method: EM (single particle) / Resolution: 23.2 Å

PDB-5vxv:
Peroxisomal membrane protein PEX15
Method: X-RAY DIFFRACTION / Resolution: 1.55 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • Saccharomyces cerevisiae (brewer's yeast)
  • saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
KeywordsMEMBRANE PROTEIN / alpha helical

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