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

• 永田, 崇

• 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

抄録

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.

収録刊行物

• Cell Reports

  Cell Reports 18 (11), 2651-2663, 2017-03-14

  Elsevier BV

キーワード

• translation initiation
• ribosome
• eIF5
• eIF3
• eIF1
• start codon selection
• ribosomal pre-initiation complex

詳細情報

• CRID: 1050282810828604288
• NII論文ID: 120006358788
• ISSN: 22111247
• HANDLE: 2433/227736
• 本文言語コード: en
• 資料種別: journal article
• データソース種別:
  • IRDB
  • CiNii Articles