期刊
ELIFE
卷 7, 期 -, 页码 -出版社
ELIFE SCIENCES PUBLICATIONS LTD
DOI: 10.7554/eLife.39273
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资金
- Medical Research Council [MC_U105184332]
- Wellcome Trust [WT096570]
- Agouron Institute
- Department of Science and Technology, Ministry of Science and Technology [Int/NZ/P-2/13]
- National Institutes of Health [GM62128]
- Human Frontier Science Program [RGP-0028/2009]
- MRC [MC_U105184332] Funding Source: UKRI
In eukaryotic translation initiation, AUG recognition of the mRNA requires accommodation of Met-tRNA(i) in a 'PIN' state, which is antagonized by the factor eIF1. eIF5 is a GTPase activating protein (GAP) of eIF2 that additionally promotes stringent AUG selection, but the molecular basis of its dual function was unknown. We present a cryo-electron microscopy (cryo-EM) reconstruction of a yeast 48S pre-initiation complex (PIC), at an overall resolution of 3.0 angstrom, featuring the N-terminal domain (NTD) of eIF5 bound to the 40S subunit at the location vacated by eIF1. eIF5 interacts with and allows a more accommodated orientation of Met-tRNAi. Substitutions of eIF5 residues involved in the eIF5-NTD/tRNAi interaction influenced initiation at near-cognate UUG codons in vivo, and the closed/open PIC conformation in vitro, consistent with direct stabilization of the codon:anticodon duplex by the wild-type eIF5-NTD. The present structure reveals the basis for a key role of eIF5 in start-codon selection.
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