Movement of elongation factor G between compact and extended conformations.
Movement of elongation factor G between compact and extended conformations.
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DOI：
10.1016/j.jmb.2014.11.010
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发表时间：
2015-01-30
影响因子：
5.6
通讯作者：
Ermolenko, Dmitri N.
中科院分区：
文献类型：
--
作者：
Salsi, Enea;Farah, Elie;Netter, Zoe;Dann, Jillian;Ermolenko, Dmitri N.
Previous structural studies suggested that ribosomal translocation is accompanied by large interdomain rearrangements of elongation factor G (EF-G). Here, we follow the movement of domain IV of EF-G relative to domain II of EF-G using ensemble and single-molecule Förster resonance energy transfer (smFRET). Our results indicate that ribosome-free EF-G predominantly adopts a compact conformation that can also, albeit infrequently, transition into a more extended conformation in which domain IV moves away from domain II. By contrast, ribosome-bound EF-G predominantly adopts an extended conformation regardless of whether it is interacting with pre- or posttranslocation ribosomes. Our data suggest that ribosome-bound EF-G may also occasionally sample at least one more compact conformation. GTP hydrolysis catalyzed by EF-G does not affect the relative stability of the observed conformations in ribosome-free and ribosome-bound EF-G. Our data support a model suggesting that, upon binding to a pretranslocation ribosome, EF-G moves from a compact to a more extended conformation. This transition is not coupled to, but likely precedes both GTP hydrolysis and mRNA/tRNA translocation.
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