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Translocation of proteins into mitochondria.
TLDR
This review summarizes the present knowledge on the import and sorting of mitochondrial precursor proteins, with a special emphasis on unresolved questions and topics of current research. Expand
A Disulfide Relay System in the Intermembrane Space of Mitochondria that Mediates Protein Import
TLDR
It is suggested that the existence of a disulfide exchange system in the IMS is unexpected in view of the free exchange of metabolites between IMS and cytosol via porin channels, and reflects the evolutionary origin of the I MS from the periplasmic space of the prokaryotic ancestors of mitochondria. Expand
COPII–cargo interactions direct protein sorting into ER-derived transport vesicles
TLDR
The results indicate that cargo packaging signals and soluble cargo adaptors are recognized by a recruitment complex comprising Sar1–GTP and Sec23/24. Expand
Erp1p and Erp2p, partners for Emp24p and Erv25p in a yeast p24 complex.
TLDR
Six new members of the yeast p24 family have been identified and characterized, and genetic and biochemical studies demonstrate that Erp1p and Erp2p function in a heteromeric complex with Emp24p andErv25p. Expand
Mitochondrial Disulfide Relay: Redox-regulated Protein Import into the Intermembrane Space*
TLDR
Although structurally unrelated, the mitochondrial disulfide relay functionally resembles the Dsb (disufide bond) system of the bacterial periplasm, the compartment from which the IMS was derived 2 billion years ago. Expand
Mitochondrial disulfide bond formation is driven by intersubunit electron transfer in Erv1 and proofread by glutathione.
TLDR
A role for a glutathione-dependent proofreading during oxidative protein folding by the mitochondrial disulfide relay is suggested by the reconstituted process in vitro using purified cytochrome c, Erv1, Mia40, and Cox19. Expand
The disulfide relay system of mitochondria is connected to the respiratory chain
TLDR
It is shown that Erv1 passes its electrons on to molecular oxygen via interaction with cy tochrome c and cytochrome c oxidase and this connection to the respiratory chain increases the efficient oxidation of the relay system in mitochondria and prevents the formation of toxic hydrogen peroxide. Expand
Ribosome binding to the Oxa1 complex facilitates co‐translational protein insertion in mitochondria
TLDR
It is shown that the matrix‐exposed C‐terminus of Oxa1 forms an α‐helical domain that has the ability to bind to mitochondrial ribosomes, suggesting that co‐translational membrane insertion of mitochondrial translation products is facilitated by a physical interaction of translation complexes with the membrane‐bound translocase. Expand
AAA proteases with catalytic sites on opposite membrane surfaces comprise a proteolytic system for the ATP‐dependent degradation of inner membrane proteins in mitochondria.
TLDR
Two AAA proteases with their catalytic sites on opposite membrane surfaces constitute a novel proteolytic system for the degradation of membrane proteins in mitochondria. Expand
Oxa1p, an essential component of the N-tail protein export machinery in mitochondria.
TLDR
It is demonstrated here that imported nuclear encoded proteins physically interact with Oxa1p and depend on Oxa2p for efficient export of their N termini to the intermembrane space, including the fully synthesized pCoxII and CoxIII species. Expand
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