| GRAF, M., P. HUTER, C. MARACCI, Miroslav PETEREK, M.V. RODNINA and D.N. WILSON. Visualization of translation termination intermediates trapped by the Apidaecin 137 peptide during RF3-mediated recycling of RF1. Nature Communications. London: Nature Publishing Group, 2018, vol. 9, AUG, p. 3053-3063. ISSN 2041-1723. Available from: https://dx.doi.org/10.1038/s41467-018-05465-1. |
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@article{1507057,
author = {Graf, M. and Huter, P. and Maracci, C. and Peterek, Miroslav and Rodnina, M.V. and Wilson, D.N.},
article_location = {London},
article_number = {AUG},
doi = {http://dx.doi.org/10.1038/s41467-018-05465-1},
keywords = {RELEASE FACTOR RF3; ELONGATION-FACTOR-G; STOP CODON RECOGNITION; ESCHERICHIA-COLI; CRYSTAL-STRUCTURE; ELECTRON CRYOMICROSCOPY; GTPASE ACTIVATION; GGQ MOTIF; CRYO-EM; EF-G},
language = {eng},
issn = {2041-1723},
journal = {Nature Communications},
title = {Visualization of translation termination intermediates trapped by the Apidaecin 137 peptide during RF3-mediated recycling of RF1},
volume = {9},
year = {2018}
}
TY - JOUR
ID - 1507057
AU - Graf, M. - Huter, P. - Maracci, C. - Peterek, Miroslav - Rodnina, M.V. - Wilson, D.N.
PY - 2018
TI - Visualization of translation termination intermediates trapped by the Apidaecin 137 peptide during RF3-mediated recycling of RF1
JF - Nature Communications
VL - 9
IS - AUG
SP - 3053
EP - 3053
PB - Nature Publishing Group
SN - 20411723
KW - RELEASE FACTOR RF3
KW - ELONGATION-FACTOR-G
KW - STOP CODON RECOGNITION
KW - ESCHERICHIA-COLI
KW - CRYSTAL-STRUCTURE
KW - ELECTRON CRYOMICROSCOPY
KW - GTPASE ACTIVATION
KW - GGQ MOTIF
KW - CRYO-EM
KW - EF-G
N2 - During translation termination in bacteria, the release factors RF1 and RF2 are recycled from the ribosome by RF3. While high-resolution structures of the individual termination factors on the ribosome exist, direct structural insight into how RF3 mediates dissociation of the decoding RFs has been lacking. Here we have used the Apidaecin 137 peptide to trap RF1 together with RF3 on the ribosome and visualize an ensemble of termination intermediates using cryo-electron microscopy. Binding of RF3 to the ribosome induces small subunit (SSU) rotation and swivelling of the head, yielding intermediate states with shifted P-site tRNAs and RF1 conformations. RF3 does not directly eject RF1 from the ribosome, but rather induces full rotation of the SSU that indirectly dislodges RF1 from its binding site. SSU rotation is coupled to the accommodation of the GTPase domain of RF3 on the large subunit (LSU), thereby promoting GTP hydrolysis and dissociation of RF3 from the ribosome.
ER -
GRAF, M., P. HUTER, C. MARACCI, Miroslav PETEREK, M.V. RODNINA and D.N. WILSON. Visualization of translation termination intermediates trapped by the Apidaecin 137 peptide during RF3-mediated recycling of RF1. \textit{Nature Communications}. London: Nature Publishing Group, 2018, vol.~9, AUG, p.~3053-3063. ISSN~2041-1723. Available from: https://dx.doi.org/10.1038/s41467-018-05465-1.
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