2ogh
From Proteopedia
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Solution structure of yeast eIF1
Overview
eIF1 is a small protein (12 kDa) governing fidelity in translation, initiation. It is recruited to the 40S 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 80S 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 (NTT) and at a basic/hydrophobic surface area, termed KH, distinct from the ribosome-binding face. Genetic and, biochemical studies indicate that eIF1-NTT 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 (Genes Dev 21, 1217). 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 40S, subunit.
About this Structure
2OGH is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Eukaryotic initiation factor (eIF) 1 carries two distinct EIF5-binding faces important for multifactor assembly and AUG selection., Reibarkh M, Yamamoto Y, Singh CR, Del Rio F, Fahmy A, Lee B, Luna RE, Wagner G, Asano K, J Biol Chem. 2007 Nov 1;. PMID:17974565
Page seeded by OCA on Wed Jan 23 10:41:51 2008
