Further Evidence that Elongation Factor 1 Remains Bound to Ribosomes during Peptide Chain Elongation
نویسندگان
چکیده
منابع مشابه
Sequence-dependent elongation dynamics on macrolide-bound ribosomes.
The traditional view of macrolide antibiotics as plugs inside the ribosomal nascent peptide exit tunnel (NPET) has lately been challenged in favor of a more complex, heterogeneous mechanism, where drug-peptide interactions determine the fate of a translating ribosome. To investigate these highly dynamic processes, we applied single-molecule tracking of elongating ribosomes during inhibition of ...
متن کاملMitotic modulation of translation elongation factor 1 leads to hindered tRNA delivery to ribosomes.
Translation elongation in eukaryotes is mediated by the concerted actions of elongation factor 1A (eEF1A), which delivers aminoacylated tRNA to the ribosome; elongation factor 1B (eEF1B) complex, which catalyzes the exchange of GDP to GTP on eEF1A; and eEF2, which facilitates ribosomal translocation. Here we present evidence in support of a novel mode of translation regulation by hindered tRNA ...
متن کاملDissimilarity 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 (EP-2). The third factor (EF-3) requirement was observed with EFs from either yeast or liver for both poly(U)-directed polyphenylalani...
متن کاملDissimilarity 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 کاملCotranslational response to proteotoxic stress by elongation pausing of ribosomes.
Translational control permits cells to respond swiftly to a changing environment. Rapid attenuation of global protein synthesis under stress conditions has been largely ascribed to the inhibition of translation initiation. Here we report that intracellular proteotoxic stress reduces global protein synthesis by halting ribosomes on transcripts during elongation. Deep sequencing of ribosome-prote...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1977
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1977.tb11787.x