Control of Ribosomal Subunit Rotation by Elongation Factor G
نویسندگان
چکیده
منابع مشابه
Control of phosphate release from elongation factor G by ribosomal protein L7/12.
Ribosomal protein L7/12 is crucial for the function of elongation factor G (EF-G) on the ribosome. Here, we report the localization of a site in the C-terminal domain (CTD) of L7/12 that is critical for the interaction with EF-G. Single conserved surface amino acids were replaced in the CTD of L7/12. Whereas mutations in helices 5 and 6 had no effect, replacements of V66, I69, K70, and R73 in h...
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 کاملStimulation of the GTPase activity of translation elongation factor G by ribosomal protein L7/12.
Elongation factors (EFs) Tu and G are GTPases that have important functions in protein synthesis. The low intrinsic GTPase activity of both factors is strongly stimulated on the ribosome by unknown mechanisms. Here we report that isolated ribosomal protein L7/12 strongly stimulates GTP hydrolysis by EF-G, but not by EF-Tu, indicating a major contribution of L7/12 to GTPase activation of EF-G on...
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15 صفحه اولFollowing movement of domain IV of elongation factor G during ribosomal translocation.
Translocation of mRNA and tRNAs through the ribosome is catalyzed by a universally conserved elongation factor (EF-G in prokaryotes and EF-2 in eukaryotes). Previous studies have suggested that ribosome-bound EF-G undergoes significant structural rearrangements. Here, we follow the movement of domain IV of EF-G, which is critical for the catalysis of translocation, relative to protein S12 of th...
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ژورنال
عنوان ژورنال: Science
سال: 2013
ISSN: 0036-8075,1095-9203
DOI: 10.1126/science.1235970