Structure of the Translation Preinitiation Complex from Wheat Germ Extract

Translation preinitiation complexes are typical components of the cytoplasm of eukaryotic cells, consisting of 40S ribosomal subunits bound to initiation factors. Actively studied in mammals and protozoa, these complexes are involved in the initiation of mRNA translation. We studied the abundance and structure of plant preinitiation complexes using single particle cryo-EM analysis of wheat germ extract preparations. Approximately 29% of free 40S subunits form a complex with the initiation factors eIF3 and eIF1A. The structure of the complex was reconstructed with overall resolution better than 3 Å and the core of factor eIF3 with a resolution of 3.6 Å. These are the first data on the structure of initiation ribosomal complex in plants. We constructed the atomic models of the iIF3 core and distal subunits; these models had notable differences comparing to those in mammalian cells.

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Publication Details

Journal
Moscow University Biological Sciences Bulletin
Published
2025-12-01
DOI
https://doi.org/10.3103/s0096392525601145
Citations
1
Primary Topic
RNA and protein synthesis mechanisms
Type
article
Field-Weighted Citation Impact
0.81
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article

Structure of the Translation Preinitiation Complex from Wheat Germ Extract

Y. A. Chesnokov, Zh. A. Afonina, O. V. Kravchenko, K. S. Vassilenko
1 citations
Moscow University Biological Sciences Bulletin
RNA and protein synthesis mechanisms
0.81
article

Structure of the Translation Preinitiation Complex from Wheat Germ Extract

Y. A. Chesnokov, Zh. A. Afonina, O. V. Kravchenko, K. S. Vassilenko
article en
1 citations

Abstract

Translation preinitiation complexes are typical components of the cytoplasm of eukaryotic cells, consisting of 40S ribosomal subunits bound to initiation factors. Actively studied in mammals and protozoa, these complexes are involved in the initiation of mRNA translation. We studied the abundance and structure of plant preinitiation complexes using single particle cryo-EM analysis of wheat germ extract preparations. Approximately 29% of free 40S subunits form a complex with the initiation factors eIF3 and eIF1A. The structure of the complex was reconstructed with overall resolution better than 3 Å and the core of factor eIF3 with a resolution of 3.6 Å. These are the first data on the structure of initiation ribosomal complex in plants. We constructed the atomic models of the iIF3 core and distal subunits; these models had notable differences comparing to those in mammalian cells.

Moscow University Biological Sciences BulletinVol. 80(S1)
Kurchatov Institute (RU), Institute of Protein Research (RU)
Life in Land
Openalex Percentile: Top 20%
RNA and protein synthesis mechanisms
0.81
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