Faculty Collaboration Database

Truncation of the Mrp20 protein reveals new ribosome-assembly subcomplex in mitochondria. EMBO Rep 2011 Sep 01;12(9):950-5

Date

07/23/2011

Pubmed ID

21779004

Pubmed Central ID

PMC3166459

DOI

10.1038/embor.2011.133

Scopus ID

2-s2.0-80052299547 (requires institutional sign-in at Scopus site)   25 Citations

Abstract

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 RA

Author

Rosemary Stuart PhD Professor in the Biology department at Marquette University

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

Membrane Proteins
Mitochondria
Mitochondrial Membranes
Mitochondrial Proteins
Oxidative Phosphorylation
Peroxiredoxins
Ribosomal Proteins
Ribosomes
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins
Sequence Deletion