2OGH

Solution structure of yeast eIF1

2OGH の概要

• エントリーDOI: 10.2210/pdb2ogh/pdb
• 分子名称: Eukaryotic translation initiation factor eIF-1 (1 entity in total)
• 機能のキーワード: alpha-beta protein, translation
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12330.15

構造登録者

Reibarkh, M.,del Rio, F.,Yamamoto, Y.,Asano, K.,Wagner, G. (登録日: 2007-01-05, 公開日: 2007-11-20, 最終更新日: 2023-12-27)

主引用文献

Reibarkh, M.,Yamamoto, Y.,Singh, C.R.,Del Rio, F.,Fahmy, A.,Lee, B.,Luna, R.E.,Ii, M.,Wagner, G.,Asano, K.
Eukaryotic Initiation Factor (eIF) 1 Carries Two Distinct eIF5-binding Faces Important for Multifactor Assembly and AUG Selection.
J.Biol.Chem., 283:1094-1103, 2008

PubMed Abstract: Eukaryotic initiation factor (eIF) 1 is a small protein (12 kDa) governing fidelity in translation initiation. It is recruited to the 40 S subunit in a multifactor complex with Met-tRNA(i)(Met), eIF2, eIF3, and eIF5 and binds near the P-site. eIF1 release in response to start codon recognition is an important signal to produce an 80 S initiation complex. Although the ribosome-binding face of eIF1 was identified, interfaces to other preinitiation complex components and their relevance to eIF1 function have not been determined. Exploiting the solution structure of yeast eIF1, here we locate the binding site for eIF5 in its N-terminal tail and at a basic/hydrophobic surface area termed KH, distinct from the ribosome-binding face. Genetic and biochemical studies indicate that the eIF1 N-terminal tail plays a stimulatory role in cooperative multifactor assembly. A mutation altering the basic part of eIF1-KH is lethal and shows a dominant phenotype indicating relaxed start codon selection. Cheung et al. recently demonstrated that the alteration of hydrophobic residues of eIF1 disrupts a critical link to the preinitiation complex that suppresses eIF1 release before start codon selection (Cheung, Y.-N., Maag, D., Mitchell, S. F., Fekete, C. A., Algire, M. A., Takacs, J. E., Shirokikh, N., Pestova, T., Lorsch, J. R., and Hinnebusch, A. (2007) Genes Dev. 21, 1217-1230 ). Interestingly, eIF1-KH includes the altered hydrophobic residues. Thus, eIF5 is an excellent candidate for the direct partner of eIF1-KH that mediates the critical link. The direct interaction at eIF1-KH also places eIF5 near the decoding site of the 40 S subunit.

PubMed: 17974565
DOI: 10.1074/jbc.M708155200

実験手法

SOLUTION NMR