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10.1016/j.celrep.2017.02.052

http://scihub22266oqcxt.onion/10.1016/j.celrep.2017.02.052
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C5382721!5382721!28297669
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suck abstract from ncbi


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pmid28297669      Cell+Rep 2017 ; 18 (11): 2651-63
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  • Molecular landscape of the ribosome pre-initiation complex during mRNA scanning: structural role for eIF3c and its control by eIF5 #MMPMID28297669
  • Obayashi E; Luna RE; Nagata T; Martin-Marcos P; Hiraishi H; Singh CR; Erzberger JP; Zhang F; Arthanari H; Morris J; Pellarin R; Moore C; Harmon I; Papadopoulos E; Yoshida H; Nasr ML; Unzai S; Thompson B; Aube E; Hustak S; Stengel F; Dagraca E; Ananbandam A; Gao P; Urano T; Hinnebusch AG; Wagner G; Asano K
  • Cell Rep 2017[Mar]; 18 (11): 2651-63 PMID28297669show ga
  • During eukaryotic translation initiation, eIF3 binds the solvent-accessible side of the 40S ribosome and recruits the gate-keeper protein eIF1 and eIF5 to the decoding center. This is largely mediated by the N-terminal domain (NTD) of eIF3c, which can be divided into three parts: 3c0, 3c1 and 3c2. The N-terminal part, 3c0, binds eIF5 strongly, but only weakly to the ribosome-binding surface of eIF1, whereas 3c1 and 3c2 form a stoichiometric complex with eIF1. 3c1 contacts eIF1 through Arg-53 and Leu-96, while 3c2 faces 40S protein uS15/S13, to anchor eIF1 to the scanning pre-initiation complex (PIC). We propose that the 3c0:eIF1 interaction diminishes eIF1 binding to the 40S, whereas 3c0:eIF5 interaction stabilizes the scanning PIC by precluding this inhibitory interaction. Upon start codon recognition, interactions involving eIF5, and ultimately 3c0:eIF1 association facilitate eIF1 release. Our results reveal intricate molecular interactions within the PIC, programmed for rapid scanning-arrest at the start codon.
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