A core of three amino acids at the carboxyl-terminal region of glutamine synthetase defines its regulation in cyanobacteria

© 2015 John Wiley & Sons Ltd. Glutamine synthetase (GS) type I is a key enzyme in nitrogen metabolism, and its activity is finely controlled by cellular carbon/nitrogen balance. In cyanobacteria, a reversible process that involves protein-protein interaction with two proteins, the inactivating f...

Descripción completa

Detalles Bibliográficos
Autores: Saelices, Lorena, Robles-Rengel, Rocío, Florencio, Francisco J., Muro-Pastor, M. Isabel
Tipo de recurso: artículo
Fecha de publicación:2015
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/115414
Acceso en línea:http://hdl.handle.net/10261/115414
Access Level:acceso abierto
Palabra clave:Synechocystis 6803
Posttranscriptional Regulation
Inactivating Factors
Glutamine Synthetase
Protein-Protein Interaction
id ES_ca2d855bf14d143e35406f9c55cf6367
oai_identifier_str oai:digital.csic.es:10261/115414
network_acronym_str ES
network_name_str España
repository_id_str
spelling A core of three amino acids at the carboxyl-terminal region of glutamine synthetase defines its regulation in cyanobacteriaSaelices, LorenaRobles-Rengel, RocíoFlorencio, Francisco J.Muro-Pastor, M. IsabelSynechocystis 6803Posttranscriptional RegulationInactivating FactorsGlutamine SynthetaseProtein-Protein Interaction© 2015 John Wiley & Sons Ltd. Glutamine synthetase (GS) type I is a key enzyme in nitrogen metabolism, and its activity is finely controlled by cellular carbon/nitrogen balance. In cyanobacteria, a reversible process that involves protein-protein interaction with two proteins, the inactivating factors IF7 and IF17, regulates GS. Previously, we showed that three arginine residues of IFs are critical for binding and inhibition of GS. In this work, taking advantage of the specificity of GS/IFs interaction in the model cyanobacteria Synechocystis sp. PCC 6803 and Anabaena sp. PCC 7120, we have constructed a different chimeric GSs from these two cyanobacteria. Analysis of these proteins, together with a site-directed mutagenesis approach, indicates that a core of three residues (E419, N456 and R459) is essential for the inactivation process. The three residues belong to the last 56 amino acids of the C-terminus of SynechocystisGS. A protein-protein docking modeling of SynechocystisGS in complex with IF7 supports the role of the identified core for GS/IF interaction.Peer ReviewedBlackwell Publishing2015201520152015info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501http://hdl.handle.net/10261/115414reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglésinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/1154142026-05-22T06:33:51Z
dc.title.none.fl_str_mv A core of three amino acids at the carboxyl-terminal region of glutamine synthetase defines its regulation in cyanobacteria
title A core of three amino acids at the carboxyl-terminal region of glutamine synthetase defines its regulation in cyanobacteria
spellingShingle A core of three amino acids at the carboxyl-terminal region of glutamine synthetase defines its regulation in cyanobacteria
Saelices, Lorena
Synechocystis 6803
Posttranscriptional Regulation
Inactivating Factors
Glutamine Synthetase
Protein-Protein Interaction
title_short A core of three amino acids at the carboxyl-terminal region of glutamine synthetase defines its regulation in cyanobacteria
title_full A core of three amino acids at the carboxyl-terminal region of glutamine synthetase defines its regulation in cyanobacteria
title_fullStr A core of three amino acids at the carboxyl-terminal region of glutamine synthetase defines its regulation in cyanobacteria
title_full_unstemmed A core of three amino acids at the carboxyl-terminal region of glutamine synthetase defines its regulation in cyanobacteria
title_sort A core of three amino acids at the carboxyl-terminal region of glutamine synthetase defines its regulation in cyanobacteria
dc.creator.none.fl_str_mv Saelices, Lorena
Robles-Rengel, Rocío
Florencio, Francisco J.
Muro-Pastor, M. Isabel
author Saelices, Lorena
author_facet Saelices, Lorena
Robles-Rengel, Rocío
Florencio, Francisco J.
Muro-Pastor, M. Isabel
author_role author
author2 Robles-Rengel, Rocío
Florencio, Francisco J.
Muro-Pastor, M. Isabel
author2_role author
author
author
dc.subject.none.fl_str_mv Synechocystis 6803
Posttranscriptional Regulation
Inactivating Factors
Glutamine Synthetase
Protein-Protein Interaction
topic Synechocystis 6803
Posttranscriptional Regulation
Inactivating Factors
Glutamine Synthetase
Protein-Protein Interaction
description © 2015 John Wiley & Sons Ltd. Glutamine synthetase (GS) type I is a key enzyme in nitrogen metabolism, and its activity is finely controlled by cellular carbon/nitrogen balance. In cyanobacteria, a reversible process that involves protein-protein interaction with two proteins, the inactivating factors IF7 and IF17, regulates GS. Previously, we showed that three arginine residues of IFs are critical for binding and inhibition of GS. In this work, taking advantage of the specificity of GS/IFs interaction in the model cyanobacteria Synechocystis sp. PCC 6803 and Anabaena sp. PCC 7120, we have constructed a different chimeric GSs from these two cyanobacteria. Analysis of these proteins, together with a site-directed mutagenesis approach, indicates that a core of three residues (E419, N456 and R459) is essential for the inactivation process. The three residues belong to the last 56 amino acids of the C-terminus of SynechocystisGS. A protein-protein docking modeling of SynechocystisGS in complex with IF7 supports the role of the identified core for GS/IF interaction.
publishDate 2015
dc.date.none.fl_str_mv 2015
2015
2015
2015
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
format article
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/115414
url http://hdl.handle.net/10261/115414
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Blackwell Publishing
publisher.none.fl_str_mv Blackwell Publishing
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
_version_ 1869419457206550528
score 15,811543

Similares en LA Referencia