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Structural basis for+1 ribosomal frameshifting during EF-G-catalyzed translocation

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F21%3A00119665" target="_blank" >RIV/00216224:14740/21:00119665 - isvavai.cz</a>

  • Result on the web

    <a href="https://www.nature.com/articles/s41467-021-24911-1" target="_blank" >https://www.nature.com/articles/s41467-021-24911-1</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1038/s41467-021-24911-1" target="_blank" >10.1038/s41467-021-24911-1</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Structural basis for+1 ribosomal frameshifting during EF-G-catalyzed translocation

  • Original language description

    Frameshifting of mRNA during translation provides a strategy to expand the coding repertoire of cells and viruses. How and where in the elongation cycle +1-frameshifting occurs remains poorly understood. We describe seven similar to 3.5-angstrom-resolution cryo-EM structures of 70S ribosome complexes, allowing visualization of elongation and translocation by the GTPase elongation factor G (EF-G). Four structures with a + 1-frameshifting-prone mRNA reveal that frameshifting takes place during translocation of tRNA and mRNA. Prior to EF-G binding, the pre-translocation complex features an in-frame tRNA-mRNA pairing in the A site. In the partially translocated structure with EF-G center dot GDPCP, the tRNA shifts to the +1-frame near the P site, rendering the freed mRNA base to bulge between the P and E sites and to stack on the 16S rRNA nucleotide G926. The ribosome remains frameshifted in the nearly post-translocation state. Our findings demonstrate that the ribosome and EF-G cooperate to induce +1 frameshifting during tRNA-mRNA translocation.

  • 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

    <a href="/en/project/GJ20-16013Y" target="_blank" >GJ20-16013Y: Simultaneous gene transcription and translation</a><br>

  • 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

    12

  • Pages from-to

    4644

  • UT code for WoS article

    000684299000001

  • EID of the result in the Scopus database

    2-s2.0-85111641609