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Mgr3p and Mgr1p are adaptors for the mitochondrial i-AAA protease complex.

ABSTRACT: By screening yeast knockouts for their dependence upon the mitochondrial genome, we identified Mgr3p, a protein that associates with the i-AAA protease complex in the mitochondrial inner membrane. Mgr3p and Mgr1p, another i-AAA-interacting protein, form a subcomplex that bind to the i-AAA subunit Yme1p. We find that loss of Mgr3p, like the lack of Mgr1p, reduces proteolysis by Yme1p. Mgr3p and Mgr1p can bind substrate even in the absence of Yme1p, and both proteins are needed for maximal binding of an unfolded substrate by the i-AAA complex. We speculate that Mgr3p and Mgr1p function in an adaptor complex that targets substrates to the i-AAA protease for degradation.

SUBMITTER: Dunn CD

PROVIDER: S-EPMC2592643 | biostudies-literature | 2008 Dec

REPOSITORIES: biostudies-literature

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Mgr3p and Mgr1p are adaptors for the mitochondrial i-AAA protease complex.

Dunn Cory D CD Tamura Yasushi Y Sesaki Hiromi H Jensen Robert E RE

Molecular biology of the cell 20081008 12

By screening yeast knockouts for their dependence upon the mitochondrial genome, we identified Mgr3p, a protein that associates with the i-AAA protease complex in the mitochondrial inner membrane. Mgr3p and Mgr1p, another i-AAA-interacting protein, form a subcomplex that bind to the i-AAA subunit Yme1p. We find that loss of Mgr3p, like the lack of Mgr1p, reduces proteolysis by Yme1p. Mgr3p and Mgr1p can bind substrate even in the absence of Yme1p, and both proteins are needed for maximal binding ...[more]

PMID: 18843051

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