MrpL35, a mitospecific component of mitoribosomes, plays a key role in cytochrome c oxidase assembly. Mol Biol Cell 2017 Nov 15;28(24):3489-3499
Date
09/22/2017Pubmed ID
28931599Pubmed Central ID
PMC5683760DOI
10.1091/mbc.E17-04-0239Scopus ID
2-s2.0-85034114272 (requires institutional sign-in at Scopus site) 31 CitationsAbstract
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.
Author List
Box JM, Kaur J, Stuart RAAuthor
Rosemary Stuart PhD Professor in the Biology department at Marquette UniversityMESH terms used to index this publication - Major topics in bold
Electron Transport Complex IVMembrane Proteins
Mitochondria
Mitochondrial Proteins
Mitochondrial Ribosomes
Oxidative Phosphorylation
Protein Biosynthesis
Protein Conformation
Protein Structural Elements
Ribosomal Proteins
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins
Transcription Factors
