Time-resolved cryo-EM visualizes ribosomal translocation with EF-G and GTP
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F21%3A00119653" target="_blank" >RIV/00216224:14740/21:00119653 - isvavai.cz</a>
Result on the web
<a href="https://www.nature.com/articles/s41467-021-27415-0" target="_blank" >https://www.nature.com/articles/s41467-021-27415-0</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1038/s41467-021-27415-0" target="_blank" >10.1038/s41467-021-27415-0</a>
Alternative languages
Result language
angličtina
Original language name
Time-resolved cryo-EM visualizes ribosomal translocation with EF-G and GTP
Original language description
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.
Czech name
—
Czech description
—
Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
—
OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2021
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Nature Communications
ISSN
2041-1723
e-ISSN
—
Volume of the periodical
12
Issue of the periodical within the volume
1
Country of publishing house
DE - GERMANY
Number of pages
13
Pages from-to
„7236“
UT code for WoS article
000729942300007
EID of the result in the Scopus database
2-s2.0-85121309324