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Elongation factor G undergoes an extensive structural rearrangement during ribosomal translocation (752.3)
Author(s) -
Ermolenko Dmitri,
Salsi Enea,
Farah Elie
Publication year - 2014
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.28.1_supplement.752.3
Subject(s) - chromosomal translocation , ribosome , ribosomal rna , protein subunit , transfer rna , p site , elongation factor , chemistry , 50s , elongation , biology , microbiology and biotechnology , biophysics , biochemistry , rna , gene , materials science , ultimate tensile strength , metallurgy
Translocation of mRNA and tRNAs through the ribosome is catalyzed by the universally conserved elongation factor (EF‐G in prokaryotes and EF‐2 in eukaryotes). It has been hypothesized that EF‐G undergoes structural rearrangements during translocation. Here, we test this hypothesis by following the movement of EF‐G relative to the small ribosomal subunit using single‐molecule Förster resonance energy transfer (smFRET). We show that ribosome‐bound EF‐G adopts distinct conformations corresponding to the pre‐ and post‐translocation states of the ribosome. Our results suggest that upon ribosomal translocation, domain IV of EF‐G, which is essential for the catalysis of translocation, moves toward the A site of the small ribosomal subunit and promotes translocation of peptidyl‐tRNA. Grant Funding Source : These studies were supported by grant from the US National Institute of Health no. GM‐099719