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Impaired folding of the mitochondrial small TIM chaperones induces clearance by the i-AAA protease.

Abstract：

:The intermembrane space of mitochondria contains a dedicated chaperone network-the small translocase of the inner membrane (TIM) family-for the sorting of hydrophobic precursors. All small TIMs are defined by the presence of a twin CX(3)C motif and the monomeric proteins are stabilized by two intramolecular disulfide bonds formed between the cysteines of these motifs. The conserved cysteine residues within small TIM members have also been shown to participate in early biogenesis events, with the most N-terminal cysteine residue important for import and retention within the intermembrane space via the receptor and disulfide oxidase, Mia40. In this study, we have analyzed the in vivo consequences of improper folding of small TIM chaperones by generating site-specific cysteine mutants and assessed the fate of the incompletely oxidized proteins within mitochondria. We show that no individual cysteine residue is required for the function of Tim9 or Tim10 in yeast and that defective assembly of the small TIMs induces their proteolytic clearance from mitochondria. We delineate a clearance mechanism for the mutant proteins and their unassembled wild-type partner protein by the mitochondrial ATP-dependent protease, Yme1 (yeast mitochondrial escape 1).

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Baker MJ,Mooga VP,Guiard B,Langer T,Ryan MT,Stojanovski D

doi

10.1016/j.jmb.2012.09.019

subject

Has Abstract

pub_date

2012-12-14 00:00:00

pages

227-39

issue

5

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(12)00784-X

journal_volume

424

pub_type

杂志文章

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