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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