Ribosomal Translocation: LepA Does It Backwards
نویسندگان
چکیده
منابع مشابه
Ribosomal Translocation: LepA Does It Backwards
During translation, mRNA is threaded through the ribosome in precise and directional three-nucleotide steps. A recent paper identifies a new GTPase, LepA, which catalyzes unexpected one-codon backward movement on the ribosome.
متن کاملThe structure of LepA, the ribosomal back translocase.
LepA is a highly conserved elongation factor that promotes the back translocation of tRNAs on the ribosome during the elongation cycle. We have determined the crystal structure of LepA from Escherichia coli at 2.8-A resolution. The high degree of sequence identity between LepA and EF-G is reflected in the structural similarity between the individual homologous domains of LepA and EF-G. However,...
متن کاملThe stoichiometry of ribosomal translocation.
Fusidic acid does not inhibit the translocation of N-acetylphenylalanyl-tRNA (N-acetyl-Phe-tRNA), bound nonenzymitally to the ribosomal A-site, when the amount of ribosomes in the reaction mixture is not sufficient to trap all the available elongation factor G (EF-G) in the form of GDP ‘EF-G .fusidic acid .ribosome complexes. Moreover, since only those ribosomes in the reaction mixture that are...
متن کاملDoes backwards induction imply subgame perfection?
In finite games subgame perfect equilibria are precisely those that are obtained by a backwards induction procedure. In large extensive form games with perfect information this equivalence does not hold: Strategy combinations fulfilling the backwards induction criterion may not be subgame perfect in general. The full equivalence is restored only under additional (topological) assumptions. This ...
متن کاملThe Highly Conserved LepA Is a Ribosomal Elongation Factor that Back-Translocates the Ribosome
The ribosomal elongation cycle describes a series of reactions prolonging the nascent polypeptide chain by one amino acid and driven by two universal elongation factors termed EF-Tu and EF-G in bacteria. Here we demonstrate that the extremely conserved LepA protein, present in all bacteria and mitochondria, is a third elongation factor required for accurate and efficient protein synthesis. LepA...
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ژورنال
عنوان ژورنال: Current Biology
سال: 2007
ISSN: 0960-9822
DOI: 10.1016/j.cub.2006.12.029