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Structural analysis of an eIF3 subcomplex reveals conserved interactions required for a stable and proper translation pre-initiation complex assembly

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F12%3A00379099" target="_blank" >RIV/61388971:_____/12:00379099 - isvavai.cz</a>

  • Result on the web

    <a href="http://dx.doi.org/10.1093/nar/gkr765" target="_blank" >http://dx.doi.org/10.1093/nar/gkr765</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1093/nar/gkr765" target="_blank" >10.1093/nar/gkr765</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Structural analysis of an eIF3 subcomplex reveals conserved interactions required for a stable and proper translation pre-initiation complex assembly

  • Original language description

    Translation initiation factor eIF3 acts as the key orchestrator of the canonical initiation pathway in eukaryotes, yet its structure is greatly unexplored. We report the 2.2 A resolution crystal structure of the complex between the yeast seven-bladed beta-propeller eIF3i/TIF34 and a C-terminal alpha-helix of eIF3b/PRT1, which reveals universally conserved interactions. Mutating these interactions displays severe growth defects and eliminates association of eIF3i/TIF34 and strikingly also eIF3g/TIF35 with eIF3 and 40S subunits in vivo. Unexpectedly, 40S-association of the remaining eIF3 subcomplex and eIF5 is likewise destabilized resulting in formation of aberrant pre-initiation complexes (PICs) containing eIF2 and eIF1, which critically compromises scanning arrest on mRNA at its AUG start codon suggesting that the contacts between mRNA and ribosomal decoding site are impaired

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

Result continuities

  • Project

  • Continuities

    Z - Vyzkumny zamer (s odkazem do CEZ)

Others

  • Publication year

    2012

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Nucleic Acids Research

  • ISSN

    0305-1048

  • e-ISSN

  • Volume of the periodical

    40

  • Issue of the periodical within the volume

    5

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    18

  • Pages from-to

    2294-2311

  • UT code for WoS article

    000302019900041

  • EID of the result in the Scopus database