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Molecular Architecture of the 40S⋅eIF1⋅eIF3 Translation Initiation Complex

Authors: Erzberger Jan P; Stengel Florian; Pellarin Riccardo; Zhang Suyang; Schaefer Tanja; Aylett Christopher H S; Cimermancic Peter; +4 Authors

Molecular Architecture of the 40S⋅eIF1⋅eIF3 Translation Initiation Complex

Abstract

Eukaryotic translation initiation requires the recruitment of the large, multiprotein eIF3 complex to the 40S ribosomal subunit. We present X-ray structures of all major components of the minimal, six-subunit Saccharomyces cerevisiae eIF3 core. These structures, together with electron microscopy reconstructions, cross-linking coupled to mass spectrometry, and integrative structure modeling, allowed us to position and orient all eIF3 components on the 40S⋅eIF1 complex, revealing an extended, modular arrangement of eIF3 subunits. Yeast eIF3 engages 40S in a clamp-like manner, fully encircling 40S to position key initiation factors on opposite ends of the mRNA channel, providing a platform for the recruitment, assembly, and regulation of the translation initiation machinery. The structures of eIF3 components reported here also have implications for understanding the architecture of the mammalian 43S preinitiation complex and the complex of eIF3, 40S, and the hepatitis C internal ribosomal entry site RNA.

ISSN:0092-8674

ISSN:1097-4172

Cell, 158 (5)

Keywords

Models, Molecular, Saccharomyces cerevisiae Proteins, Eukaryotic Initiation Factor-3, Molecular Sequence Data, Eukaryotic Initiation Factor-1, Hepacivirus, Saccharomyces cerevisiae, Crystallography, X-Ray, Article, Animals, Humans, Amino Acid Sequence, Peptide Chain Initiation, Translational, info:eu-repo/classification/ddc/570, Mammals, Ribosome Subunits, Small, Eukaryotic, Biochemistry, Genetics and Molecular Biology(all), Microscopy, Electron, Ribonucleoproteins, Dimerization, Sequence Alignment

  • BIP!
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    citations
    This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
    203
    popularity
    This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
    Top 1%
    influence
    This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
    Top 10%
    impulse
    This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
    Top 1%
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citations
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
203
Top 1%
Top 10%
Top 1%
Green
hybrid