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@article{1834781,
author = {Carbone, C.E. and Loveland, A.B. and Gamper, H.B. and Hou, Y.M. and Demo, Gabriel and Korostelev, A.A.},
article_location = {London},
article_number = {1},
doi = {http://dx.doi.org/10.1038/s41467-021-27415-0},
keywords = {ELONGATION-FACTOR-GTRANSFER-RNA TRANSLOCATIONCONFORMATIONAL-CHANGESINTERSUBUNIT MOVEMENTINTERMEDIATE STATESCRYSTAL-STRUCTURESTRUCTURAL BASISHYBRID STATE80S RIBOSOMEHYDROLYSIS},
language = {eng},
issn = {2041-1723},
journal = {Nature Communications},
title = {Time-resolved cryo-EM visualizes ribosomal translocation with EF-G and GTP},
url = {https://www.nature.com/articles/s41467-021-27415-0},
volume = {12},
year = {2021}
}
TY - JOUR
ID - 1834781
AU - Carbone, C.E. - Loveland, A.B. - Gamper, H.B. - Hou, Y.M. - Demo, Gabriel - Korostelev, A.A.
PY - 2021
TI - Time-resolved cryo-EM visualizes ribosomal translocation with EF-G and GTP
JF - Nature Communications
VL - 12
IS - 1
SP - „7236“
EP - „7236“
PB - Nature Publishing Group
SN - 20411723
KW - ELONGATION-FACTOR-GTRANSFER-RNA TRANSLOCATIONCONFORMATIONAL-CHANGESINTERSUBUNIT MOVEMENTINTERMEDIATE STATESCRYSTAL-STRUCTURESTRUCTURAL BASISHYBRID STATE80S RIBOSOMEHYDROLYSIS
UR - https://www.nature.com/articles/s41467-021-27415-0
N2 - During translation, a conserved GTPase elongation factor-EF-G in bacteria or eEF2 in eukaryotes-translocates tRNA and mRNA through the ribosome. EF-G has been proposed to act as a flexible motor that propels tRNA and mRNA movement, as a rigid pawl that biases unidirectional translocation resulting from ribosome rearrangements, or by various combinations of motor- and pawl-like mechanisms. Using time-resolved cryo-EM, we visualized GTP-catalyzed translocation without inhibitors, capturing elusive structures of ribosome.EF-G intermediates at near-atomic resolution. Prior to translocation, EF-G binds near peptidyl-tRNA, while the rotated 30S subunit stabilizes the EF-G GTPase center. Reverse 30S rotation releases Pi and translocates peptidyl-tRNA and EF-G by similar to 20 angstrom. An additional 4-angstrom translocation initiates EF-G dissociation from a transient ribosome state with highly swiveled 30S head. The structures visualize how nearly rigid EF-G rectifies inherent and spontaneous ribosomal dynamics into tRNA-mRNA translocation, whereas GTP hydrolysis and Pi release drive EF-G dissociation.
ER -
CARBONE, C.E., A.B. LOVELAND, H.B. GAMPER, Y.M. HOU, Gabriel DEMO a A.A. KOROSTELEV. Time-resolved cryo-EM visualizes ribosomal translocation with EF-G and GTP. \textit{Nature Communications}. London: Nature Publishing Group, 2021, roč.~12, č.~1, s.~„7236“, 13 s. ISSN~2041-1723. Dostupné z: https://dx.doi.org/10.1038/s41467-021-27415-0.
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