Structure-function analysis of Escherichia coli MnmG (GidA), a highly conserved tRNA-modifying enzyme

The MnmE-MnmG complex is involved in tRNA modification. We have determined the crystal structure of Escherichia coli MnmG at 2.4-A resolution, mutated highly conserved residues with putative roles in flavin adenine dinucleotide (FAD) or tRNA binding and MnmE interaction, and analyzed the effects of...

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Detalles Bibliográficos
Autores: Shi, Rong, Villarroya, Magda, Ruiz-Partida, Rafael, Li, Yunge, Proteau, Ariane, Prado, Silvia, Moukadiri, Ismaïl, Benítez-Páez, Alfonso, Lomas, Rodrigo, Wagner, John, Matte, Allan, Velázquez-Campoy, Adrián, Armengod, M-Eugenia, Cygler, Miroslaw
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2009
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/344983
Acceso en línea:http://hdl.handle.net/10261/344983
https://api.elsevier.com/content/abstract/scopus_id/72449211907
Access Level:acceso abierto
Palabra clave:Escherichia coli
MnmG
tRNA modification
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spelling Structure-function analysis of Escherichia coli MnmG (GidA), a highly conserved tRNA-modifying enzymeShi, RongVillarroya, MagdaRuiz-Partida, RafaelLi, YungeProteau, ArianePrado, SilviaMoukadiri, IsmaïlBenítez-Páez, AlfonsoLomas, RodrigoWagner, JohnMatte, AllanVelázquez-Campoy, AdriánArmengod, M-EugeniaCygler, MiroslawEscherichia coliMnmGtRNA modificationThe MnmE-MnmG complex is involved in tRNA modification. We have determined the crystal structure of Escherichia coli MnmG at 2.4-A resolution, mutated highly conserved residues with putative roles in flavin adenine dinucleotide (FAD) or tRNA binding and MnmE interaction, and analyzed the effects of these mutations in vivo and in vitro. Limited trypsinolysis of MnmG suggests significant conformational changes upon FAD binding.This work was supported by grant GSP-48370 from the Canadian Institutes of Health Research (to M.C. and A.M.) and grant BFU2007-66509 from the Ministerio de Ciencia e Innovación (to M.-E.A.).Peer reviewedAmerican Society for MicrobiologyCanadian Institutes of Health ResearchMinisterio de Ciencia e Innovación (España)#NODATA##NODATA##NODATA##NODATA##NODATA##NODATA##NODATA##NODATA##NODATA##NODATA##NODATA##NODATA##NODATA##NODATA#202420242009info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/344983https://api.elsevier.com/content/abstract/scopus_id/72449211907reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglés#PLACEHOLDER_PARENT_METADATA_VALUE#info:eu-repo/grantAgreement/MEC//BFU2007-66509Journal of bacteriologyhttps://doi.org/10.1128/jb.00650-09Noinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/3449832026-05-22T06:33:51Z
dc.title.none.fl_str_mv Structure-function analysis of Escherichia coli MnmG (GidA), a highly conserved tRNA-modifying enzyme
title Structure-function analysis of Escherichia coli MnmG (GidA), a highly conserved tRNA-modifying enzyme
spellingShingle Structure-function analysis of Escherichia coli MnmG (GidA), a highly conserved tRNA-modifying enzyme
Shi, Rong
Escherichia coli
MnmG
tRNA modification
title_short Structure-function analysis of Escherichia coli MnmG (GidA), a highly conserved tRNA-modifying enzyme
title_full Structure-function analysis of Escherichia coli MnmG (GidA), a highly conserved tRNA-modifying enzyme
title_fullStr Structure-function analysis of Escherichia coli MnmG (GidA), a highly conserved tRNA-modifying enzyme
title_full_unstemmed Structure-function analysis of Escherichia coli MnmG (GidA), a highly conserved tRNA-modifying enzyme
title_sort Structure-function analysis of Escherichia coli MnmG (GidA), a highly conserved tRNA-modifying enzyme
dc.creator.none.fl_str_mv Shi, Rong
Villarroya, Magda
Ruiz-Partida, Rafael
Li, Yunge
Proteau, Ariane
Prado, Silvia
Moukadiri, Ismaïl
Benítez-Páez, Alfonso
Lomas, Rodrigo
Wagner, John
Matte, Allan
Velázquez-Campoy, Adrián
Armengod, M-Eugenia
Cygler, Miroslaw
author Shi, Rong
author_facet Shi, Rong
Villarroya, Magda
Ruiz-Partida, Rafael
Li, Yunge
Proteau, Ariane
Prado, Silvia
Moukadiri, Ismaïl
Benítez-Páez, Alfonso
Lomas, Rodrigo
Wagner, John
Matte, Allan
Velázquez-Campoy, Adrián
Armengod, M-Eugenia
Cygler, Miroslaw
author_role author
author2 Villarroya, Magda
Ruiz-Partida, Rafael
Li, Yunge
Proteau, Ariane
Prado, Silvia
Moukadiri, Ismaïl
Benítez-Páez, Alfonso
Lomas, Rodrigo
Wagner, John
Matte, Allan
Velázquez-Campoy, Adrián
Armengod, M-Eugenia
Cygler, Miroslaw
author2_role author
author
author
author
author
author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Canadian Institutes of Health Research
Ministerio de Ciencia e Innovación (España)
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#NODATA#
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#NODATA#
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dc.subject.none.fl_str_mv Escherichia coli
MnmG
tRNA modification
topic Escherichia coli
MnmG
tRNA modification
description The MnmE-MnmG complex is involved in tRNA modification. We have determined the crystal structure of Escherichia coli MnmG at 2.4-A resolution, mutated highly conserved residues with putative roles in flavin adenine dinucleotide (FAD) or tRNA binding and MnmE interaction, and analyzed the effects of these mutations in vivo and in vitro. Limited trypsinolysis of MnmG suggests significant conformational changes upon FAD binding.
publishDate 2009
dc.date.none.fl_str_mv 2009
2024
2024
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Publisher's version
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/344983
https://api.elsevier.com/content/abstract/scopus_id/72449211907
url http://hdl.handle.net/10261/344983
https://api.elsevier.com/content/abstract/scopus_id/72449211907
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv #PLACEHOLDER_PARENT_METADATA_VALUE#
info:eu-repo/grantAgreement/MEC//BFU2007-66509
Journal of bacteriology
https://doi.org/10.1128/jb.00650-09
No
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv American Society for Microbiology
publisher.none.fl_str_mv American Society for Microbiology
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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