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Truncation of the Mrp20 protein reveals new ribosome‐assembly subcomplex in mitochondria
Author(s) -
Kaur Jasvinder,
Stuart Rosemary A
Publication year - 2011
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/embor.2011.133
Subject(s) - mitochondrion , ribosome , microbiology and biotechnology , truncation (statistics) , biology , computational biology , computer science , biochemistry , rna , gene , machine learning
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 mrp20 Δ C yeast mutant. Finally, data supporting the idea that the inner mitochondrial membrane acts as a platform for the ribosome assembly process are discussed.