Journal
JOURNAL OF CELL BIOLOGY
Volume 214, Issue 4, Pages 417-431Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.201602074
Keywords
-
Categories
Funding
- Deutsche Forschungsgemeinschaft [IRTG1830, SPP1710]
- BioComp-Forschungsschwerpunkt Rheinland-Pfalz
- Spanish Ministerio de Ciencia e Innovacion [BFU2008-000475]
- Junta de Extremadura-European Social Fund [GR10108]
Ask authors/readers for more resources
Tim17 is a central, membrane-embedded subunit of the mitochondrial protein import machinery. In this study, we show that Tim17 contains a pair of highly conserved cysteine residues that form a structural disulfide bond exposed to the intermembrane space (IMS). This disulfide bond is critical for efficient protein translocation through the TIM23 complex and for dynamic gating of its preprotein-conducting channel. The disulfide bond in Tim17 is formed during insertion of the protein into the inner membrane. Whereas the import of Tim17 depends on the binding to the IMS protein Mia40, the oxidoreductase activity of Mia40 is surprisingly dispensable for Tim17 oxidation. Our observations suggest that Tim17 can be directly oxidized by the sulfhydryl oxidase Erv1. Thus, import and oxidation of Tim17 are mediated by the mitochondrial disulfide relay, though the mechanism by which the disulfide bond in Tim17 is formed differs considerably from that of soluble IMS proteins.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available