MrpL35, a mitospecific component of mitoribosomes, plays a key role in cytochrome
| Autor: | Jodie M, Box, Jasvinder, Kaur, Rosemary A, Stuart |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
Ribosomal Proteins
Saccharomyces cerevisiae Proteins Protein Conformation Biosynthesis and Biodegradation Membrane Proteins Saccharomyces cerevisiae Articles Oxidative Phosphorylation Mitochondria Electron Transport Complex IV Mitochondrial Proteins Mitochondrial Ribosomes Protein Biosynthesis Protein Structural Elements Transcription Factors |
| Zdroj: | Molecular Biology of the Cell |
| ISSN: | 1939-4586 |
| Popis: | MrpL35 and Mrp7, components of the mitoribosome, play a role in regulating the COX assembly process and influence the molecular environments of the Mss51, Coa3, and Cox14 proteins, chaperones involved in posttranslational assembly events for the COX complex. Mitoribosomes perform the synthesis of the core components of the oxidative phosphorylation (OXPHOS) system encoded by the mitochondrial genome. We provide evidence that MrpL35 (mL38), a mitospecific component of the yeast mitoribosomal central protuberance, assembles into a subcomplex with MrpL7 (uL5), Mrp7 (bL27), and MrpL36 (bL31) and mitospecific proteins MrpL17 (mL46) and MrpL28 (mL40). We isolated respiratory defective mrpL35 mutant yeast strains, which do not display an overall inhibition in mitochondrial protein synthesis but rather have a problem in cytochrome c oxidase complex (COX) assembly. Our findings indicate that MrpL35, with its partner Mrp7, play a key role in coordinating the synthesis of the Cox1 subunit with its assembly into the COX enzyme and in a manner that involves the Cox14 and Coa3 proteins. We propose that MrpL35 and Mrp7 are regulatory subunits of the mitoribosome acting to coordinate protein synthesis and OXPHOS assembly events and thus the bioenergetic capacity of the mitochondria. |
| Databáze: | OpenAIRE |
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