Reference - Detail
|Author||Woogeng IN, Kitakawa M.|
|Title||The C-terminal extension domain of Saccharomyces cerevisiae MrpL32, a homolog of ribosomal protein L32, functions in trans to support mitochondrial translation.|
|Journal||Genes Genet. Syst.|
Mitochondrial ribosomal protein L32 (MrpL32) of Saccharomyces cerevisiae is homologous to the bacterial L32 ribosomal protein. MrpL32 carries an N-terminal mitochondrion-targeting sequence (MTS) and is about 60 amino acid residues longer at the C-terminus. Adding to its function as a leader sequence, the MTS of MrpL32 has been reported to regulate ribosome biogenesis through its processing by m-AAA protease. However, the function of the C-terminal extension (CE) remains totally unknown. Therefore, we constructed a series of C-terminally truncated mrpl32 (mrpl32ΔC) genes and expressed them in a Δmrpl32 mutant to examine their function. Interestingly, some MrpL32ΔC derivatives exhibited temperature-sensitive (ts) growth on medium with non-fermentable carbon sources. Furthermore, the CE domain of MrpL32, expressed separately from MrpL32ΔC, could rescue the ts phenotype of mutants by improving mitochondrial protein synthesis.
|MeSH||5' Untranslated Regions Culture Media Metalloendopeptidases / metabolism Mitochondria / metabolism* Mitochondrial Proteins / metabolism Mutation* Protein Biosynthesis Protein Domains Protein Sorting Signals Ribosomal Proteins / chemistry* Ribosomal Proteins / genetics Ribosomal Proteins / metabolism* Ribosomes / metabolism Saccharomyces cerevisiae / chemistry Saccharomyces cerevisiae / genetics Saccharomyces cerevisiae / growth & development* Saccharomyces cerevisiae / metabolism Saccharomyces cerevisiae Proteins / chemistry* Saccharomyces cerevisiae Proteins / genetics Saccharomyces cerevisiae Proteins / metabolism* Temperature|