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Mrpl36 is important for generation of assembly competent proteins during mitochondrial translation

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Item Type:Article
Title:Mrpl36 is important for generation of assembly competent proteins during mitochondrial translation
Creators Name:Prestele, M. and Vogel, F. and Reichert, A.S. and Herrmann, J.M. and Ott, M.
Abstract:The complexes of the respiratory chain represent mosaics of nuclear and mitochondrially encoded components. The processes by which synthesis and assembly of the various subunits are coordinated remain largely elusive. During evolution, many proteins of the mitochondrial ribosome acquired additional domains pointing at specific properties or functions of the translation machinery in mitochondria. Here, we analyzed the function of Mrpl36, a protein associated with the large subunit of the mitochondrial ribosome. This protein, homologous to the ribosomal protein L31 from bacteria, contains a mitochondria-specific C-terminal domain that is not required for protein synthesis per se; however, its absence decreases stability of Mrpl36. Cells lacking this C-terminal domain can still synthesize proteins, but these translation products fail to be properly assembled into respiratory chain complexes and are rapidly degraded. Surprisingly, overexpression of Mrpl36 seems to even increase the efficiency of mitochondrial translation. Our data suggest that Mrpl36 plays a critical role during translation that determines the rate of respiratory chain assembly. This important function seems to be carried out by a stabilizing activity of Mrpl36 on the interaction between large and small ribosomal subunits, which could influence accuracy of protein synthesis.
Keywords:GTP Phosphohydrolases, Mitochondria, Mitochondrial Proteins, Biological Models, Mutation, Protein Binding, Protein Biosynthesis, Protein Stability, Tertiary Protein Structure, Ribosomal Proteins, Ribosomes, Saccharomyces Cerevisiae, Saccharomyces Cerevisiae Proteins, Solubility
Source:Molecular Biology of the Cell
ISSN:1059-1524
Publisher:American Society for Cell Biology (U.S.A.)
Volume:20
Number:10
Page Range:2615-2625
Date:May 2009
Official Publication:https://doi.org/10.1091/mbc.E08-12-1162
PubMed:View item in PubMed

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