Perez-Martinez X, et al. (2009) Dual Functions of Mss51 Couple Synthesis of Cox1 to Assembly of Cytochrome c Oxidase in Saccharomyces cerevisiae Mitochondria. Mol Biol Cell 20(20):4371-80
Abstract: Monitoring Editor: Janet M. Shaw Functional interactions of the translational activator Mss51 with both the mitochondrially encoded COX1 mRNA 5'-UTR and with newly synthesized unassembled Cox1 protein suggest that it has a key role in coupling Cox1 synthesis with assembly of cytochrome c oxidase. Mss51 is present at levels that are near-rate-limiting for expression of a reporter gene inserted at COX1 in mtDNA, and a substantial fraction of Mss51 is associated with Cox1 protein in assembly intermediates. Thus, sequestration of Mss51 in assembly intermediates could limit Cox1 synthesis in wild-type, and account for the reduced Cox1 synthesis caused by most yeast mutations that block assembly. Mss51 does not stably interact with newly synthesized Cox1 in a mutant lacking Cox14, suggesting that the failure of nuclear cox14 mutants to decrease Cox1 synthesis, despite their inability to assemble cytochrome c oxidase, is due to a failure to sequester Mss51. The physical interaction between Mss51 and Cox14 is dependent upon Cox1 synthesis, indicating dynamic assembly of early cytochrome c oxidase intermediates nucleated by Cox1. Regulation of COX1 mRNA translation by Mss51 appears to be an example of a homeostatic mechanism in which a positive effector of gene expression interacts with the product it regulates in a post-translational assembly process.
|Status: Published||Type: Journal Article||PubMed ID: 19710419|
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|DNA/RNA Sequence Features|
|Protein-Nucleic Acid Interactions|