Position of Eukaryotic Translation Initiation Factor eIF1A on the 40S Ribosomal Subunit Mapped by Directed Hydroxyl Radical Probing

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dc.contributor.author Yu, Yingpu en_US
dc.contributor.author Marintchev, Assen en_US
dc.contributor.author Kolupaeva, Victoria G. en_US
dc.contributor.author Unbehaun, Anett en_US
dc.contributor.author Veryasova, Tatyana en_US
dc.contributor.author Lai, Shao-Chiang en_US
dc.contributor.author Hong, Peng en_US
dc.contributor.author Wagner, Gerhard en_US
dc.contributor.author Hellen, Christopher U. T. en_US
dc.contributor.author Pestova, Tatyana V. en_US
dc.date.accessioned 2012-01-12T17:34:26Z
dc.date.available 2012-01-12T17:34:26Z
dc.date.copyright 2009 en_US
dc.date.issued 2009-8 en_US
dc.identifier.citation Yu, Yingpu, Assen Marintchev, Victoria G. Kolupaeva, Anett Unbehaun, Tatyana Veryasova, Shao-Chiang Lai, Peng Hong, Gerhard Wagner, Christopher U. T. Hellen, Tatyana V. Pestova. "Position of eukaryotic translation initiation factor eIF1A on the 40S ribosomal subunit mapped by directed hydroxyl radical probing" Nucleic Acids Research 37(15): 5167-5182. (2009) en_US
dc.identifier.issn 1362-4962 en_US
dc.identifier.uri http://hdl.handle.net/2144/3399
dc.description.abstract The universally conserved eukaryotic initiation factor (eIF), eIF1A, plays multiple roles throughout initiation: it stimulates eIF2/GTP/Met-tRNAiMet attachment to 40S ribosomal subunits, scanning, start codon selection and subunit joining. Its bacterial ortholog IF1 consists of an oligonucleotide/oligosaccharide-binding (OB) domain, whereas eIF1A additionally contains a helical subdomain, N-terminal tail (NTT) and C-terminal tail (CTT). The NTT and CTT both enhance ribosomal recruitment of eIF2/GTP/Met-tRNAiMet, but have opposite effects on the stringency of start codon selection: the CTT increases, whereas the NTT decreases it. Here, we determined the position of eIF1A on the 40S subunit by directed hydroxyl radical cleavage. eIF1A's OB domain binds in the A site, similar to IF1, whereas the helical subdomain contacts the head, forming a bridge over the mRNA channel. The NTT and CTT both thread under Met-tRNAiMet reaching into the P-site. The NTT threads closer to the mRNA channel. In the proposed model, the NTT does not clash with either mRNA or Met-tRNAiMet, consistent with its suggested role in promoting the 'closed' conformation of ribosomal complexes upon start codon recognition. In contrast, eIF1A-CTT appears to interfere with the P-site tRNA-head interaction in the 'closed' complex and is likely ejected from the P-site upon start codon recognition. en_US
dc.description.sponsorship National Institutes of Health (GM59660, GM47467, CA68268); National Cancer Institute (Howard Temin award K01 CA119107); Boston University (Peter Paul Career Development Professorship award) en_US
dc.language.iso en en_US
dc.rights Copyright 2009 Yu, Yingpu, Assen Marintchev, Victoria G. Kolupaeva, Anett Unbehaun, Tatyana Veryasova, Shao-Chiang Lai, Peng Hong, Gerhard Wagner, Christopher U. T. Hellen, Tatyana V. Pestova en_US
dc.rights.uri http://creativecommons.org/licenses/by-nc/2.0/uk/ en_US
dc.title Position of Eukaryotic Translation Initiation Factor eIF1A on the 40S Ribosomal Subunit Mapped by Directed Hydroxyl Radical Probing en_US
dc.type article en_US
dc.identifier.doi 10.1093/nar/gkp519 en_US
dc.identifier.pubmedid 19561193 en_US
dc.identifier.pmcid 2731904 en_US

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