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Vol. 19, Issue 12, 5387-5397, December 2008
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Department of Cell Biology, The Johns Hopkins University School of Medicine, Baltimore, MD 21205
Submitted February 1, 2008;
Revised September 12, 2008;
Accepted September 29, 2008
Monitoring Editor: Peter Walter
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.
* Present address: Department of Biochemistry and Molecular Biophysics, Howard Hughes Medical Institute, Columbia University College of Physicians and Surgeons, 701 West 168th St., Room 720, New York, NY 10032.
Address correspondence to: Robert Jensen (rjensen{at}jhmi.edu).
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