Ontology highlight
ABSTRACT:
SUBMITTER: Dunn CD
PROVIDER: S-EPMC2592643 | biostudies-literature | 2008 Dec
REPOSITORIES: biostudies-literature
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]