A structural inventory of native ribosomal ABCE1‐43S pre‐initiation complexes |
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Authors: | Hanna Kratzat Timur MackensKiani Michael Ameismeier Mia Potocnjak Jingdong Cheng Estelle Dacheux Abdelkader Namane Otto Berninghausen Franz Herzog Micheline FromontRacine Thomas Becker Roland Beckmann |
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Institution: | 1. Gene Center and Center for Integrated Protein Science Munich, Department of Biochemistry, University of Munich, Munich Germany ; 2. Génétique des Interactions Macromoléculaires, UMR3525 CNRS, Institut Pasteur, Paris France |
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Abstract: | In eukaryotic translation, termination and ribosome recycling phases are linked to subsequent initiation of a new round of translation by persistence of several factors at ribosomal sub‐complexes. These comprise/include the large eIF3 complex, eIF3j (Hcr1 in yeast) and the ATP‐binding cassette protein ABCE1 (Rli1 in yeast). The ATPase is mainly active as a recycling factor, but it can remain bound to the dissociated 40S subunit until formation of the next 43S pre‐initiation complexes. However, its functional role and native architectural context remains largely enigmatic. Here, we present an architectural inventory of native yeast and human ABCE1‐containing pre‐initiation complexes by cryo‐EM. We found that ABCE1 was mostly associated with early 43S, but also with later 48S phases of initiation. It adopted a novel hybrid conformation of its nucleotide‐binding domains, while interacting with the N‐terminus of eIF3j. Further, eIF3j occupied the mRNA entry channel via its ultimate C‐terminus providing a structural explanation for its antagonistic role with respect to mRNA binding. Overall, the native human samples provide a near‐complete molecular picture of the architecture and sophisticated interaction network of the 43S‐bound eIF3 complex and the eIF2 ternary complex containing the initiator tRNA. |
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Keywords: | ABCE1 eIF3 cryo‐ EM translation initiation ribosome recycling |
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