Proteomics

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Receptor-mediated recruitment of cytosolic J-proteins to the mitochondrial outer membrane promotes assembly of preprotein translocases


ABSTRACT: Mitochondria possess elaborate machineries for the import of preproteins from the cytosol. Cytosolic factors like Hsp70 chaperones and their co-chaperones, the J-proteins, guide preproteins to the mitochondrial surface. The translocase of the mitochondrial outer membrane (TOM) forms the entry gate for precursor proteins. How proteins are delivered to the receptors Tom20, Tom22 and Tom70 is only understood in part. We identified the cytosolic J-protein Xdj1 as a specific interaction partner of the central receptor Tom22. Tom22 recruits Xdj1 to the mitochondrial surface to promote assembly of the TOM complex. A second J-protein of the cytosol, Djp1, binds to Tom70 to mediate biogenesis of the mitochondrial import (MIM) complex. Thus, by targeting distinct TOM receptors, cytosolic J-proteins promote the biogenesis of different mitochondrial preprotein translocases.

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Friedel Drepper  

LAB HEAD: Bettina Warscheid

PROVIDER: PXD008203 | Pride | 2018-11-26

REPOSITORIES: Pride

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Publications

Recruitment of Cytosolic J-Proteins by TOM Receptors Promotes Mitochondrial Protein Biogenesis.

Opaliński Łukasz Ł   Song Jiyao J   Priesnitz Chantal C   Wenz Lena-Sophie LS   Oeljeklaus Silke S   Warscheid Bettina B   Pfanner Nikolaus N   Becker Thomas T  

Cell reports 20181101 8


Mitochondria possess elaborate machineries for the import of proteins from the cytosol. Cytosolic factors like Hsp70 chaperones and their co-chaperones, the J-proteins, guide proteins to the mitochondrial surface. The translocase of the mitochondrial outer membrane (TOM) forms the entry gate for preproteins. How the proteins are delivered to mitochondrial preprotein receptors is poorly understood. We identify the cytosolic J-protein Xdj1 as a specific interaction partner of the central receptor  ...[more]

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