Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 23, Issue 2, Pages 125-+Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.3160
Keywords
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Funding
- Institute of Biophysics 135 Goal-oriented Project
- Key Laboratory of RNA Biology (Institute of Biophysics, Chinese Academy of Sciences)
- Ministry of Science and Technology of China [2012CB911000, 2013CB531200, 2013CB910404]
- National Natural Science Foundation of China [31322015, 31170756, 31270847, 31422016, 31470722]
- Strategic Priority Research program of the Chinese Academy of Sciences [XDB08010203]
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EF4 catalyzes tRNA back-translocation through an unknown mechanism. We report cryo-EM structures of Escherichia coli EF4 in post-and pretranslocational ribosomes (Post-and Pre-EF4) at 3.7-and 3.2-A resolution, respectively. In Post-EF4, peptidyl-tRNA occupies the peptidyl (P) site, but the interaction between its CCA end and the P loop is disrupted. In Pre-EF4, the peptidyl-tRNA assumes a unique position near the aminoacyl (A) site, denoted the A site/EF4 bound (A/4) site, with a large displacement at its acceptor arm. Mutagenesis analyses suggest that a specific region in the EF4 C-terminal domain (CTD) interferes with base-pairing between the peptidyl-tRNA 3'-CCA and the P loop, whereas the EF4 CTD enhances peptidyl-tRNA interaction at the A/4 site. Therefore, EF4 induces back-translocation by disengaging the tRNA's CCA end from the peptidyl transferase center of the translating ribosome.
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