Medical College of Wisconsin
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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



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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 RA


Rosemary Stuart PhD Professor in the Biology department at Marquette University

MESH terms used to index this publication - Major topics in bold

Electron Transport Complex IV
Membrane Proteins
Mitochondrial Proteins
Mitochondrial Ribosomes
Oxidative Phosphorylation
Protein Biosynthesis
Protein Conformation
Protein Structural Elements
Ribosomal Proteins
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins
Transcription Factors
jenkins-FCD Prod-482 91ad8a360b6da540234915ea01ff80e38bfdb40a