Mss51 and Ssc1 facilitate translational regulation of cytochrome c oxidase biogenesis.

Department of Neurology, University of Miami Miller School of Medicine, Miami, FL 33136, USA.
The intricate biogenesis of multimeric organellar enzymes of dual genetic origin entails several levels of regulation. In Saccharomyces cerevisiae, mitochondrial cytochrome c oxidase (COX) assembly is regulated translationally. Synthesis of subunit 1 (Cox1) is contingent on the availability of its assembly partners, thereby acting as a negative feedback loop that coordinates COX1 mRNA translation with Cox1 utilization during COX assembly. The COX1 mRNA-specific translational activator Mss51 plays a fundamental role in this process. Here, we report that Mss51 successively interacts with the COX1 mRNA translational apparatus, newly synthesized Cox1, and other COX assembly factors during Cox1 maturation/assembly. Notably, the mitochondrial Hsp70 chaperone Ssc1 is shown to be an Mss51 partner throughout its metabolic cycle. We conclude that Ssc1, by interacting with Mss51 and Mss51-containing complexes, plays a critical role in Cox1 biogenesis, COX assembly, and the translational regulation of these processes.
Mesh Terms:
Calcium-Transporting ATPases, Electron Transport Complex IV, Molecular Chaperones, Molecular Weight, Mutation, Protein Biosynthesis, Protein Interaction Mapping, Protein Subunits, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Transcription Factors
Mol. Cell. Biol. Jan. 01, 2010; 30(1);245-59 [PUBMED:19858289]
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