学術雑誌論文 Molecular Landscape of the Ribosome Pre-initiation Complex during mRNA Scanning: Structural Role for eIF3c and Its Control by eIF5

Obayashi, Eiji  ,  Luna, Rafael E.  ,  Nagata, Takashi  ,  Martin-Marcos, Pilar  ,  Hiraishi, Hiroyuki  ,  Singh, Chingakham Ranjit  ,  Erzberger, Jan Peter  ,  Zhang, Fan  ,  Arthanari, Haribabu  ,  Morris, Jacob  ,  Pellarin, Riccardo  ,  Moore, Chelsea  ,  Harmon, Ian  ,  Papadopoulos, Evangelos  ,  Yoshida, Hisashi  ,  Nasr, Mahmoud L.  ,  Unzai, Satoru  ,  Thompson, Brytteny  ,  Aube, Eric  ,  Hustak, Samantha  ,  Stengel, Florian  ,  Dagraca, Eddie  ,  Ananbandam, Asokan  ,  Gao, Philip  ,  Urano, Takeshi  ,  Hinnebusch, Alan G.  ,  Wagner, Gerhard  ,  Asano, Katsura

18 ( 11 )  , pp.2651 - 2663 , 2017-03-14 , Elsevier BV
ISSN:2211-1247
内容記述
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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http://repository.kulib.kyoto-u.ac.jp/dspace/bitstream/2433/227736/1/j.celrep.2017.02.052.pdf

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