Conformational Changes of Elongation Factor G on the Ribosome during tRNA Translocation
نویسندگان
چکیده
منابع مشابه
Conformational Changes of Elongation Factor G on the Ribosome during tRNA Translocation
The universally conserved GTPase elongation factor G (EF-G) catalyzes the translocation of tRNA and mRNA on the ribosome after peptide bond formation. Despite numerous studies suggesting that EF-G undergoes extensive conformational rearrangements during translocation, high-resolution structures exist for essentially only one conformation of EF-G in complex with the ribosome. Here, we report fou...
متن کاملConformational changes of the small ribosomal subunit during elongation factor G-dependent tRNA-mRNA translocation.
Translocation, a coordinated movement of two tRNAs together with mRNA on the ribosome, is catalyzed by elongation factor G (EF-G). The reaction is accompanied by conformational rearrangements of the ribosome that are, as yet, not well characterized. Here, we analyze those rearrangements by restricting the conformational flexibility of the ribosome by antibiotics binding to specific sites of the...
متن کاملLarge-Scale Movement of Elongation Factor G and Extensive Conformational Change of the Ribosome during Translocation
Elongation factor (EF) G promotes tRNA translocation on the ribosome. We present three-dimensional reconstructions, obtained by cryo-electron microscopy, of EF-G-ribosome complexes before and after translocation. In the pretranslocation state, domain 1 of EF-G interacts with the L7/12 stalk on the 50S subunit, while domain 4 contacts the shoulder of the 30S subunit in the region where protein S...
متن کاملSynchronous tRNA movements during translocation on the ribosome are orchestrated by elongation factor G and GTP hydrolysis.
The translocation of tRNAs through the ribosome proceeds through numerous small steps in which tRNAs gradually shift their positions on the small and large ribosomal subunits. The most urgent questions are: (i) whether these intermediates are important; (ii) how the ribosomal translocase, the GTPase elongation factor G (EF-G), promotes directed movement; and (iii) how the energy of GTP hydrolys...
متن کاملAn elongation factor G-induced ribosome rearrangement precedes tRNA-mRNA translocation.
The elongation cycle of protein synthesis is completed by translocation, a rearrangement during which two tRNAs bound to the mRNA move on the ribosome. The reaction is promoted by elongation factor G (EF-G) and accelerated by GTP hydrolysis. Here we report a pre-steady-state kinetic analysis of translocation. The kinetic model suggests that GTP hydrolysis drives a conformational rearrangement o...
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ژورنال
عنوان ژورنال: Cell
سال: 2015
ISSN: 0092-8674
DOI: 10.1016/j.cell.2014.11.049