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Mgr2 promotes coupling of the mitochondrial presequence translocase to partner complexes.

Authors:
Gebert M, Schrempp SG, Mehnert CS, Heißwolf AK, Oeljeklaus S, Ieva R, Bohnert M, von der Malsburg K, Wiese S, Kleinschroth T, Hunte C, Meyer HE, Haferkamp I, Guiard B, Warscheid B, Pfanner N, van der Laan M
Affiliation:
Journal:
The Journal of cell biology

Abstract

Many mitochondrial proteins are synthesized with N-terminal presequences in the cytosol. The presequence translocase of the inner mitochondrial membrane (TIM23) translocates preproteins into and across the membrane and associates with the matrix-localized import motor. The TIM23 complex consists of three core components and Tim21, which interacts with the translocase of the outer membrane (TOM) and the respiratory chain. We have identified a new subunit of the TIM23 complex, the inner membrane protein Mgr2. Mitochondria lacking Mgr2 were deficient in the Tim21-containing sorting form of the TIM23 complex. Mgr2 was required for binding of Tim21 to TIM23(CORE), revealing a binding chain of TIM23(CORE)-Mgr2/Tim21-respiratory chain. Mgr2-deficient yeast cells were defective in growth at elevated temperature, and the mitochondria were impaired in TOM-TIM23 coupling and the import of presequence-carrying preproteins. We conclude that Mgr2 is a coupling factor of the presequence translocase crucial for cell growth at elevated temperature and for efficient protein import.

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