Dissimilarity in protein chain elongation factor requirements between yeast and rat liver ribosomes.
نویسندگان
چکیده
Factor requirements for yeast and rat liver ribosomes were determined in several different reactions using either yeast or liver factors. In polymerization assays yeast ribosomes required a factor in addition to elongation factor 1 (EF-1) and elongation factor 2 (EP-2). The third factor (EF-3) requirement was observed with EFs from either yeast or liver for both poly(U)-directed polyphenylalanine synthesis and elongation of endogenous peptidyl-tRNA. No significant effect of EF-3 was observed with liver risomes in either assay. In contrast to results with polypeptide synthesis EF-3 was not required for EF-1 dependent binding of [3H]Phe-tRNA or the translocation-dependent formation of N-acetylphenylalanylpuromycin. Up to 2-fold stimulation of the binding reaction was observed with saturating levels of either yeast or liver EF-1. No effect of EF-3 was observed on ribosome-EF-2-GDP-fusidic acid complex formation. The data suggest that the yeast EF-3 may be a loosely bound ribosomal protein which is not required for a specific step in the elongation cycle but is involved in the coordination of the partial reactions required for polymerization.
منابع مشابه
Dissimilarity in Protein Chain Elongation Factor Requirements between Yeast and Rat Liver Ribosomes
Factor requirements for yeast and rat liver ribosomes were determined in several different reactions using either yeast or liver factors. In polymerization assays yeast ribosomes required a factor in addition to elongation factor 1 (EF-1) and elongation factor 2 (EF-2). The third factor (EF3) requirement was observed with EFs from either yeast or liver for both poly(U)-directed polyphenylalanin...
متن کاملProtein synthesis in yeast. Identification of an altered elongation factor in thermolabile mutants of the yeast Saccharomyces cerevisiae.
Cell-free extracts from the wild type yeast strain (A364A) and from a group of noncomplementing mutants that are conditionally defective in translation were preincubated at a restrictive temperature prior to incubation at a permissive temperature for protein synthesis. Results of these experiments showed that upon exposure to the restrictive temperature (39 degrees C), all five of the noncomple...
متن کاملCross-linking study on localization of the binding site for elongation factor 1 alpha on rat liver ribosomes.
Complexes containing rat liver 80 S ribosomes, poly(uridylic acid), phenylalanyl-tRNA, elongation factor 1 alpha, and guanylyl(beta, gamma-methylene)-diphosphonate were prepared. Neighboring proteins in the complexes were cross-linked with the bifunctional reagent 2-iminothiolane. Proteins were extracted and then separated into 26 fractions by chromatography on carboxymethylcellulose. Each prot...
متن کاملThe sensitivity of rat liver and yeast mitochondrial ribosomes to inhibitors of protein synthesis.
Amino acid incorporation by isolated intact rat liver mitochondria was severely inhibited by chloramphenicol, carbomycin, or sparsomycin, partially inhibited by emetine, and unatIected by erytbromycin or lincomycin. By contrast, amino acid incorporation by inner membrane-matrix fractions prepared from rat liver mitochondria by digitonin was strongly inhibited by emetine, erythromycin, and linco...
متن کاملAurintricarboxylic acid inhibition of the binding of phenylalanyl-tRNAa to rat liver ribosomal subunits.
Aurintricarboxylic acid (ATA) inhibits the initiation of protein synthesis in cell-free systems from both prokaryotes and eukaryotes at concentrations which do not affect chain elongation [ l-71 . We report here the effect of ATA on the poly U-dependent binding of Phe-tRNA to rat liver ribosomal subunits. ATA inhibits Phe-tRNA binding to 40 S subunits, catalysed by the rat liver cytosol initiat...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- The Journal of biological chemistry
دوره 252 4 شماره
صفحات -
تاریخ انتشار 1977