The dynamic cycle of bacterial translation initiation factor IF3

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InnovatePeru [382-PNICP-PIBA-2014 and 297INNOVATEPERU-EC-2016 to P.M.]; Fondo Nacional de Desarrollo Cientifico, Tecnologico y de Innovacion Tecnologica [154-2017-Fondecyt and 0362019-Fondecyt-BM-INC.INV to P.M.]; FIRB Futuro in Ricerca [RBFR130VS5 001 to A.F.]; Italian Ministero dell'Istruzion...

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Detalles Bibliográficos
Autores: Nakamoto, Jose A., Evangelista, Wilfredo, Vinogradova, Daria S., Konevega, Andrey L., Spurio, Roberto, Fabbretti, Attilio, Milon, Pohl
Formato: artículo
Fecha de Publicación:2021
Institución:Consejo Nacional de Ciencia Tecnología e Innovación
Repositorio:CONCYTEC-Institucional
Lenguaje:inglés
OAI Identifier:oai:repositorio.concytec.gob.pe:20.500.12390/2949
Enlace del recurso:https://hdl.handle.net/20.500.12390/2949
https://doi.org/10.1093/nar/gkab522
Nivel de acceso:acceso abierto
Materia:molecular biology
bacterial translation
https://purl.org/pe-repo/ocde/ford#3.02.18
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oai_identifier_str oai:repositorio.concytec.gob.pe:20.500.12390/2949
network_acronym_str CONC
network_name_str CONCYTEC-Institucional
repository_id_str 4689
dc.title.none.fl_str_mv The dynamic cycle of bacterial translation initiation factor IF3
title The dynamic cycle of bacterial translation initiation factor IF3
spellingShingle The dynamic cycle of bacterial translation initiation factor IF3
Nakamoto, Jose A.
molecular biology
bacterial translation
https://purl.org/pe-repo/ocde/ford#3.02.18
title_short The dynamic cycle of bacterial translation initiation factor IF3
title_full The dynamic cycle of bacterial translation initiation factor IF3
title_fullStr The dynamic cycle of bacterial translation initiation factor IF3
title_full_unstemmed The dynamic cycle of bacterial translation initiation factor IF3
title_sort The dynamic cycle of bacterial translation initiation factor IF3
author Nakamoto, Jose A.
author_facet Nakamoto, Jose A.
Evangelista, Wilfredo
Vinogradova, Daria S.
Konevega, Andrey L.
Spurio, Roberto
Fabbretti, Attilio
Milon, Pohl
author_role author
author2 Evangelista, Wilfredo
Vinogradova, Daria S.
Konevega, Andrey L.
Spurio, Roberto
Fabbretti, Attilio
Milon, Pohl
author2_role author
author
author
author
author
author
dc.contributor.author.fl_str_mv Nakamoto, Jose A.
Evangelista, Wilfredo
Vinogradova, Daria S.
Konevega, Andrey L.
Spurio, Roberto
Fabbretti, Attilio
Milon, Pohl
dc.subject.none.fl_str_mv molecular biology
topic molecular biology
bacterial translation
https://purl.org/pe-repo/ocde/ford#3.02.18
dc.subject.es_PE.fl_str_mv bacterial translation
dc.subject.ocde.none.fl_str_mv https://purl.org/pe-repo/ocde/ford#3.02.18
description InnovatePeru [382-PNICP-PIBA-2014 and 297INNOVATEPERU-EC-2016 to P.M.]; Fondo Nacional de Desarrollo Cientifico, Tecnologico y de Innovacion Tecnologica [154-2017-Fondecyt and 0362019-Fondecyt-BM-INC.INV to P.M.]; FIRB Futuro in Ricerca [RBFR130VS5 001 to A.F.]; Italian Ministero dell'Istruzione, dell'Universita e della Ricerca (to A.F.); Part of the work on structural dynamics of the ribosome was supported by Russian Science Foundation [17-1401416 to A.L.K.]. Funding for open access: Universidad Peruana de Ciencias Aplicadas (Exp-03).
publishDate 2021
dc.date.accessioned.none.fl_str_mv 2024-05-30T23:13:38Z
dc.date.available.none.fl_str_mv 2024-05-30T23:13:38Z
dc.date.issued.fl_str_mv 2021
dc.type.none.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.uri.none.fl_str_mv https://hdl.handle.net/20.500.12390/2949
dc.identifier.doi.none.fl_str_mv https://doi.org/10.1093/nar/gkab522
url https://hdl.handle.net/20.500.12390/2949
https://doi.org/10.1093/nar/gkab522
dc.language.iso.none.fl_str_mv eng
language eng
dc.relation.ispartof.none.fl_str_mv NUCLEIC ACIDS RESEARCH
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
dc.rights.uri.none.fl_str_mv https://creativecommons.org/licenses/by-nc-nd/4.0/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/4.0/
dc.publisher.none.fl_str_mv Oxford University Press
publisher.none.fl_str_mv Oxford University Press
dc.source.none.fl_str_mv reponame:CONCYTEC-Institucional
instname:Consejo Nacional de Ciencia Tecnología e Innovación
instacron:CONCYTEC
instname_str Consejo Nacional de Ciencia Tecnología e Innovación
instacron_str CONCYTEC
institution CONCYTEC
reponame_str CONCYTEC-Institucional
collection CONCYTEC-Institucional
repository.name.fl_str_mv Repositorio Institucional CONCYTEC
repository.mail.fl_str_mv repositorio@concytec.gob.pe
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spelling Publicationrp08329600rp08334600rp08330600rp08335600rp08331600rp08332600rp08333600Nakamoto, Jose A.Evangelista, WilfredoVinogradova, Daria S.Konevega, Andrey L.Spurio, RobertoFabbretti, AttilioMilon, Pohl2024-05-30T23:13:38Z2024-05-30T23:13:38Z2021https://hdl.handle.net/20.500.12390/2949https://doi.org/10.1093/nar/gkab522InnovatePeru [382-PNICP-PIBA-2014 and 297INNOVATEPERU-EC-2016 to P.M.]; Fondo Nacional de Desarrollo Cientifico, Tecnologico y de Innovacion Tecnologica [154-2017-Fondecyt and 0362019-Fondecyt-BM-INC.INV to P.M.]; FIRB Futuro in Ricerca [RBFR130VS5 001 to A.F.]; Italian Ministero dell'Istruzione, dell'Universita e della Ricerca (to A.F.); Part of the work on structural dynamics of the ribosome was supported by Russian Science Foundation [17-1401416 to A.L.K.]. Funding for open access: Universidad Peruana de Ciencias Aplicadas (Exp-03).Initiation factor IF3 is an essential protein that enhances the fidelity and speed of bacterial mRNA translation initiation. Here, we describe the dynamic interplay between IF3 domains and their alternative binding sites using pre-steady state kinetics combined with molecular modelling of available structures of initiation complexes. Our results show that IF3 accommodates its domains at velocities ranging over two orders of magnitude, responding to the binding of each 30S ligand. IF1 and IF2 promote IF3 compaction and the movement of the C-terminal domain (IF3C) towards the P site. Concomitantly, the N-terminal domain (IF3N) creates a pocket ready to accept the initiator tRNA. Selection of the initiator tRNA is accompanied by a transient accommodation of IF3N towards the 30S platform. Decoding of the mRNA start codon displaces IF3C away from the P site and rate limits translation initiation. 70S initiation complex formation brings IF3 domains in close proximity to each other prior to dissociation and recycling of the factor for a new round of translation initiation. Altogether, our results describe the kinetic spectrum of IF3 movements and highlight functional transitions of the factor that ensure accurate mRNA translation initiation.Consejo Nacional de Ciencia, Tecnología e Innovación Tecnológica - ConcytecengOxford University PressNUCLEIC ACIDS RESEARCHinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/4.0/molecular biologybacterial translation-1https://purl.org/pe-repo/ocde/ford#3.02.18-1The dynamic cycle of bacterial translation initiation factor IF3info:eu-repo/semantics/articlereponame:CONCYTEC-Institucionalinstname:Consejo Nacional de Ciencia Tecnología e Innovacióninstacron:CONCYTEC20.500.12390/2949oai:repositorio.concytec.gob.pe:20.500.12390/29492024-05-30 16:12:23.921https://creativecommons.org/licenses/by-nc-nd/4.0/info:eu-repo/semantics/openAccesshttp://purl.org/coar/access_right/c_14cbinfo:eu-repo/semantics/closedAccessmetadata only accesshttps://repositorio.concytec.gob.peRepositorio Institucional CONCYTECrepositorio@concytec.gob.pe#PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE#<Publication xmlns="https://www.openaire.eu/cerif-profile/1.1/" id="cc174ece-e136-4c1e-b3be-3bc2b609a688"> <Type xmlns="https://www.openaire.eu/cerif-profile/vocab/COAR_Publication_Types">http://purl.org/coar/resource_type/c_1843</Type> <Language>eng</Language> <Title>The dynamic cycle of bacterial translation initiation factor IF3</Title> <PublishedIn> <Publication> <Title>NUCLEIC ACIDS RESEARCH</Title> </Publication> </PublishedIn> <PublicationDate>2021</PublicationDate> <DOI>https://doi.org/10.1093/nar/gkab522</DOI> <Authors> <Author> <DisplayName>Nakamoto, Jose A.</DisplayName> <Person id="rp08329" /> <Affiliation> <OrgUnit> </OrgUnit> </Affiliation> </Author> <Author> <DisplayName>Evangelista, Wilfredo</DisplayName> <Person id="rp08334" /> <Affiliation> <OrgUnit> </OrgUnit> </Affiliation> </Author> <Author> <DisplayName>Vinogradova, Daria S.</DisplayName> <Person id="rp08330" /> <Affiliation> <OrgUnit> </OrgUnit> </Affiliation> </Author> <Author> <DisplayName>Konevega, Andrey L.</DisplayName> <Person id="rp08335" /> <Affiliation> <OrgUnit> </OrgUnit> </Affiliation> </Author> <Author> <DisplayName>Spurio, Roberto</DisplayName> <Person id="rp08331" /> <Affiliation> <OrgUnit> </OrgUnit> </Affiliation> </Author> <Author> <DisplayName>Fabbretti, Attilio</DisplayName> <Person id="rp08332" /> <Affiliation> <OrgUnit> </OrgUnit> </Affiliation> </Author> <Author> <DisplayName>Milon, Pohl</DisplayName> <Person id="rp08333" /> <Affiliation> <OrgUnit> </OrgUnit> </Affiliation> </Author> </Authors> <Editors> </Editors> <Publishers> <Publisher> <DisplayName>Oxford University Press</DisplayName> <OrgUnit /> </Publisher> </Publishers> <License>https://creativecommons.org/licenses/by-nc-nd/4.0/</License> <Keyword>molecular biology</Keyword> <Keyword>bacterial translation</Keyword> <Abstract>Initiation factor IF3 is an essential protein that enhances the fidelity and speed of bacterial mRNA translation initiation. Here, we describe the dynamic interplay between IF3 domains and their alternative binding sites using pre-steady state kinetics combined with molecular modelling of available structures of initiation complexes. Our results show that IF3 accommodates its domains at velocities ranging over two orders of magnitude, responding to the binding of each 30S ligand. IF1 and IF2 promote IF3 compaction and the movement of the C-terminal domain (IF3C) towards the P site. Concomitantly, the N-terminal domain (IF3N) creates a pocket ready to accept the initiator tRNA. Selection of the initiator tRNA is accompanied by a transient accommodation of IF3N towards the 30S platform. Decoding of the mRNA start codon displaces IF3C away from the P site and rate limits translation initiation. 70S initiation complex formation brings IF3 domains in close proximity to each other prior to dissociation and recycling of the factor for a new round of translation initiation. Altogether, our results describe the kinetic spectrum of IF3 movements and highlight functional transitions of the factor that ensure accurate mRNA translation initiation.</Abstract> <Access xmlns="http://purl.org/coar/access_right" > </Access> </Publication> -1
score 13.394457
The dynamic cycle of bacterial translation initiation factor IF3
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