Universität zu Köln

Finger, Yannik and Riemer, Jan (2020). Protein import by the mitochondrial disulfide relay in higher eukaryotes. Biol. Chem., 401 (6-7). S. 749 - 764. BERLIN: WALTER DE GRUYTER GMBH. ISSN 1437-4315

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Abstract

The proteome of the mitochondrial intermembrane space (IMS) contains more than 100 proteins, all of which are synthesized on cytosolic ribosomes and-consequently need to be imported by dedicated machineries. The mitochondrial disulfide relay is the major import machinery for soluble proteins in the IMS. Its major-component, the oxidoreductase MIA40, interacts with incoming substrates, retains them in the IMS, and oxidatively folds them. After this reaction, MIA40 is reoxidized by the sulfhydryl oxidase augmenter of liver regeneration, which couples disulfide formation by this-machinery to the activity of the respiratory chain. In this review, we will discuss the import of IMS proteins with a focus on recent findings showing the diversity of disulfide relay substrates, describing the cytosolic control of this import system and highlighting the physiological relevance of the disulfide relay machinery in higher eukaryotes.

Item Type:	Journal Article
Creators:	Creators Email ORCID ORCID Put Code Finger, Yannik UNSPECIFIED UNSPECIFIED UNSPECIFIED Riemer, Jan UNSPECIFIED UNSPECIFIED UNSPECIFIED
URN:	urn:nbn:de:hbz:38-334782
DOI:	10.1515/hsz-2020-0108
Journal or Publication Title:	Biol. Chem.
Volume:	401
Number:	6-7
Page Range:	S. 749 - 764
Date:	2020
Publisher:	WALTER DE GRUYTER GMBH
Place of Publication:	BERLIN
ISSN:	1437-4315
Language:	English
Faculty:	Faculty of Mathematics and Natural Sciences
Divisions:	Faculty of Mathematics and Natural Sciences > Department of Chemistry > Institute of Biochemistry
Subjects:	no entry
Uncontrolled Keywords:	Keywords Language INTERMEMBRANE SPACE; LIVER-REGENERATION; SULFHYDRYL OXIDASE; ELECTRON-TRANSFER; SUPEROXIDE-DISMUTASE; RESPIRATORY-CHAIN; CRYSTAL-STRUCTURE; COPPER CHAPERONE; STRUCTURAL BASIS; BOND FORMATION Multiple languages Biochemistry & Molecular Biology Multiple languages
Refereed:	Yes
URI:	http://kups.ub.uni-koeln.de/id/eprint/33478