Directional transition from initiation to elongation in bacterial translation

2.50
Hdl Handle:
http://hdl.handle.net/10757/579679
Title:
Directional transition from initiation to elongation in bacterial translation
Authors:
Goyal, Akanksha; Belardinelli, Riccardo; Maracci, Cristina; Milón, Pohl; Rodnina, Marina V.
Publisher:
Oxford University Press
Journal:
Nucleic Acids Research (Nucleic Acids Research)
Issue Date:
14-Oct-2015
URI:
http://hdl.handle.net/10757/579679
DOI:
10.1093/nar/gkv869
Additional Links:
http://nar.oxfordjournals.org/content/early/2015/09/03/nar.gkv869.full.pdf+html
Abstract:
The transition of the 30S initiation complex (IC) to the translating 70S ribosome after 50S subunit joining provides an important checkpoint for mRNA selection during translation in bacteria. Here, we study the timing and control of reactions that occur during 70S IC formation by rapid kinetic techniques, using a toolbox of fluorescence-labeled translation components. We present a kinetic model based on global fitting of time courses obtained with eight different reporters at increasing concentrations of 50S subunits. IF1 and IF3 together affect the kinetics of subunit joining, but do not alter the elemental rates of subsequent steps of 70S IC maturation. After 50S subunit joining, IF2-dependent reactions take place independent of the presence of IF1 or IF3. GTP hydrolysis triggers the efficient dissociation of fMet-tRNAfMet from IF2 and promotes the dissociation of IF2 and IF1 from the 70S IC, but does not affect IF3. The presence of non-hydrolyzable GTP analogs shifts the equilibrium towards a stable 70S–mRNA–IF1–IF2–fMet-tRNAfMet complex. Our kinetic analysis reveals the molecular choreography of the late stages in translation initiation.
Type:
info:eu-repo/semantics/article
Rights:
info:eu-repo/semantics/openAccess
Language:
eng
Keywords:
Elongation; Bacterial translation; Directional transition
ISSN:
0305-1048
EISSN:
1362-4962

Full metadata record

DC FieldValue Language
dc.contributor.authorGoyal, Akankshaes_PE
dc.contributor.authorBelardinelli, Riccardoes_PE
dc.contributor.authorMaracci, Cristinaes_PE
dc.contributor.authorMilón, Pohles_PE
dc.contributor.authorRodnina, Marina V.es_PE
dc.date.accessioned2015-10-14T18:01:25Zes_PE
dc.date.available2015-10-14T18:01:25Zes_PE
dc.date.issued2015-10-14es_PE
dc.identifier.issn0305-1048es_PE
dc.identifier.doi10.1093/nar/gkv869es_PE
dc.identifier.urihttp://hdl.handle.net/10757/579679es_PE
dc.description.abstractThe transition of the 30S initiation complex (IC) to the translating 70S ribosome after 50S subunit joining provides an important checkpoint for mRNA selection during translation in bacteria. Here, we study the timing and control of reactions that occur during 70S IC formation by rapid kinetic techniques, using a toolbox of fluorescence-labeled translation components. We present a kinetic model based on global fitting of time courses obtained with eight different reporters at increasing concentrations of 50S subunits. IF1 and IF3 together affect the kinetics of subunit joining, but do not alter the elemental rates of subsequent steps of 70S IC maturation. After 50S subunit joining, IF2-dependent reactions take place independent of the presence of IF1 or IF3. GTP hydrolysis triggers the efficient dissociation of fMet-tRNAfMet from IF2 and promotes the dissociation of IF2 and IF1 from the 70S IC, but does not affect IF3. The presence of non-hydrolyzable GTP analogs shifts the equilibrium towards a stable 70S–mRNA–IF1–IF2–fMet-tRNAfMet complex. Our kinetic analysis reveals the molecular choreography of the late stages in translation initiation.eng
dc.formatapplication/pdfes_PE
dc.language.isoenges_PE
dc.publisherOxford University Presses_PE
dc.relation.urlhttp://nar.oxfordjournals.org/content/early/2015/09/03/nar.gkv869.full.pdf+htmles_PE
dc.rightsinfo:eu-repo/semantics/openAccesses_PE
dc.sourceUniversidad Peruana de Ciencias Aplicadas (UPC)es_PE
dc.sourceRepositorio Académico - UPCes_PE
dc.subjectElongationes_PE
dc.subjectBacterial translationes_PE
dc.subjectDirectional transitiones_PE
dc.titleDirectional transition from initiation to elongation in bacterial translationes_PE
dc.typeinfo:eu-repo/semantics/articlees_PE
dc.identifier.eissn1362-4962es_PE
dc.identifier.journalNucleic Acids Research (Nucleic Acids Research)es_PE
dc.description.fundingBoehringen Ingelheim Fonds and the G¨ottingen Graduate School for Neurosciences, Biophysics, and Molecular Biosciences (to A.G.); Max Planck Society and grants of the Deutsche Forschungsgemeinschaft (to M.V.R.); Peruvian Programa Nacional de Innovaci ´on para la Competitividad y Productividad [382-PNICP-PIBA-2014 (to P.M.)]. Funding for open access charge: Max Planck Society.eng
dc.description.peer-reviewRevisión por pareses_PE
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