Truncation of the Mrp20 protein reveals new ribosome-assembly subcomplex in mitochondria. EMBO Rep 2011 Sep 01;12(9):950-5
Date
07/23/2011Pubmed ID
21779004Pubmed Central ID
PMC3166459DOI
10.1038/embor.2011.133Scopus ID
2-s2.0-80052299547 (requires institutional sign-in at Scopus site) 24 CitationsAbstract
Mitochondrial ribosomal protein 20 (Mrp20) is a component of the yeast mitochondrial large (54S) ribosomal subunit and is homologous to the bacterial L23 protein, located at the ribosomal tunnel exit site. The carboxy-terminal mitochondrial-specific domain of Mrp20 was found to have a crucial role in the assembly of the ribosomes. A new, membrane-bound, ribosomal-assembly subcomplex composed of known tunnel-exit-site proteins, an uncharacterized ribosomal protein, MrpL25, and the mitochondrial peroxiredoxin (Prx), Prx1, accumulates in an mrp20ΔC yeast mutant. Finally, data supporting the idea that the inner mitochondrial membrane acts as a platform for the ribosome assembly process are discussed.
Author List
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
Membrane ProteinsMitochondria
Mitochondrial Membranes
Mitochondrial Proteins
Oxidative Phosphorylation
Peroxiredoxins
Ribosomal Proteins
Ribosomes
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins
Sequence Deletion