dc.contributor.author | Julián Vallejo, Patricia | |
dc.contributor.author | Milon, Pohl | |
dc.contributor.author | Agirrezabala, Xabier | |
dc.contributor.author | Lasso, Gorka | |
dc.contributor.author | Gil, David | |
dc.contributor.author | Rodnina, Marina V. | |
dc.contributor.author | Valle Rodríguez, Mikel Karmel | |
dc.date.accessioned | 2013-01-22T19:31:18Z | |
dc.date.available | 2013-01-22T19:31:18Z | |
dc.date.issued | 2011-07-05 | |
dc.identifier.citation | PLoS Biol 9(7) : (2011) // e1001095 | es |
dc.identifier.issn | 1545-7885 | |
dc.identifier.uri | http://hdl.handle.net/10810/9225 | |
dc.description | 11 p. | es |
dc.description.abstract | Formation of the 30S initiation complex (30S IC) is an important checkpoint in regulation of gene expression. The selection of mRNA, correct start codon, and the initiator fMet-tRNA(fMet) requires the presence of three initiation factors (IF1, IF2, IF3) of which IF3 and IF1 control the fidelity of the process, while IF2 recruits fMet-tRNA(fMet). Here we present a cryo-EM reconstruction of the complete 30S IC, containing mRNA, fMet-tRNA(fMet), IF1, IF2, and IF3. In the 30S IC, IF2 contacts IF1, the 30S subunit shoulder, and the CCA end of fMet-tRNA(fMet), which occupies a novel P/I position (P/I1). The N-terminal domain of IF3 contacts the tRNA, whereas the C-terminal domain is bound to the platform of the 30S subunit. Binding of initiation factors and fMet-tRNA(fMet) induces a rotation of the head relative to the body of the 30S subunit, which is likely to prevail through 50S subunit joining until GTP hydrolysis and dissociation of IF2 take place. The structure provides insights into the mechanism of mRNA selection during translation initiation. | es |
dc.description.sponsorship | MV is supported by Etortek Research Program (The Department of Industry, Tourism and Trade of the Government of the Autonomous Community of the Basque Country) and from the Innovation Technology Department of the Bizkaia County. XA holds a Ramón y Cajal contract from the Ministry of Science and Technology (RYC-2009-04885). MVR and PM were supported by the Deutsche Forschungsgemeinschaft. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript. | es |
dc.language.iso | eng | es |
dc.publisher | Public Library of Science | es |
dc.rights | info:eu-repo/semantics/openAccess | es |
dc.subject | transfer-RNA selection | es |
dc.subject | factor IF2 | es |
dc.subject | messenger-RNA | es |
dc.subject | ribosomal-subunit | es |
dc.subject | protein-synthesis | es |
dc.subject | crystal-structure | es |
dc.subject | 70S ribosome | es |
dc.subject | bacillus-stearothermophilus | es |
dc.subject | conformational-changes | es |
dc.subject | angstrom resolution | es |
dc.title | The Cryo-EM Structure of a Complete 30S Translation Initiation Complex from Escherichia coli | es |
dc.type | info:eu-repo/semantics/article | es |
dc.rights.holder | © 2011 Julián et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. | es |
dc.relation.publisherversion | http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pbio.1001095 | es |
dc.identifier.doi | 10.1371/journal.pbio.1001095 | |
dc.departamentoes | Bioquímica y biología molecular | es_ES |
dc.departamentoeu | Biokimika eta biologia molekularra | es_ES |
dc.subject.categoria | AGRICULTURAL AND BIOLOGICAL SCIENCES | |
dc.subject.categoria | NEUROSCIENCES | |
dc.subject.categoria | IMMUNOLOGY AND MICROBIOLOGY | |
dc.subject.categoria | BIOCHEMISTRY AND MOLECULAR BIOLOGY | |