Literature DB >> 23810859

Reinitiation and other unconventional posttermination events during eukaryotic translation.

Maxim A Skabkin1, Olga V Skabkina, Christopher U T Hellen, Tatyana V Pestova.   

Abstract

During ribosome recycling, posttermination complexes are dissociated by ABCE1 and eRF1 into 60S and tRNA/mRNA-associated 40S subunits, after which tRNA and mRNA are released by eIF1/eIF1A, Ligatin, or MCT-1/DENR. Occasionally, 40S subunits remain associated with mRNA and reinitiate at nearby AUGs. We recapitulated reinitiation using a reconstituted mammalian translation system. The presence of eIF2, eIF3, eIF1, eIF1A, and Met-tRNAi(Met) was sufficient for recycled 40S subunits to remain on mRNA, scan bidirectionally, and reinitiate at upstream and downstream AUGs if mRNA regions flanking the stop codon were unstructured. Imposition of 3' directionality additionally required eIF4F. Strikingly, posttermination ribosomes were not stably anchored on mRNA and migrated bidirectionally to codons cognate to the P site tRNA. Migration depended on the mode of peptide release (puromycin > eRF1⋅eRF3) and nature of tRNA and was enhanced by eEF2. The mobility of posttermination ribosomes suggests that some reinitiation events could involve 80S ribosomes rather than 40S subunits.
Copyright © 2013 Elsevier Inc. All rights reserved.

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Year:  2013        PMID: 23810859      PMCID: PMC4038429          DOI: 10.1016/j.molcel.2013.05.026

Source DB:  PubMed          Journal:  Mol Cell        ISSN: 1097-2765            Impact factor:   17.970


  52 in total

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  76 in total

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5.  Crystal Structure of the C-terminal Domain of Human eIF2D and Its Implications on Eukaryotic Translation Initiation.

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6.  Structure of the 40S-ABCE1 post-splitting complex in ribosome recycling and translation initiation.

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Journal:  Nat Struct Mol Biol       Date:  2017-04-03       Impact factor: 15.369

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