Glutamine synthetase inactivation by protein-protein interaction

Glutamine synthetase (GS; EC 6.3.1.2) is the pivotal enzyme of nitrogen metabolism in prokaryotes. Control of bacterial GS activity by reversible adenylylation has provided one of the classical paradigms of signal transduction by cyclic cascades. By contrast, in the present work we show that cyanoba...

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Detalles Bibliográficos
Autores: García-Dominguez, Mario, Reyes, José C., Florencio Bellido, Francisco Javier
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:1999
País:España
Institución:Universidad de Sevilla (US)
Repositorio:idUS. Depósito de Investigación de la Universidad de Sevilla
OAI Identifier:oai:idus.us.es:11441/69683
Acceso en línea:https://hdl.handle.net/11441/69683
https://doi.org/10.1073/pnas.96.13.7161
Access Level:acceso abierto
Palabra clave:Cyanobacteria
Enzyme regulation
Nitrogen metabolism
Synechocystis 6803
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spelling Glutamine synthetase inactivation by protein-protein interactionGarcía-Dominguez, MarioReyes, José C.Florencio Bellido, Francisco JavierCyanobacteriaEnzyme regulationNitrogen metabolismSynechocystis 6803Glutamine synthetase (GS; EC 6.3.1.2) is the pivotal enzyme of nitrogen metabolism in prokaryotes. Control of bacterial GS activity by reversible adenylylation has provided one of the classical paradigms of signal transduction by cyclic cascades. By contrast, in the present work we show that cyanobacterial GS is controlled by a different mechanism that involves the interaction of two inhibitory polypeptides with the enzyme. Both inactivating factors (IFs), named IF7 and IF17, are required in vivo for complete GS inactivation. Inactive GS-IF7 and GS-IF17 complexes were reconstituted in vitro by using Escherichia coli-expressed purified proteins. Our data suggest that control of GS activity is exerted by regulating the levels of IF7 and IF17.Dirección General de Enseñanza Superior e Investigación Científica PB 94-1444Junta de Andalucía CV1-0112National Academy of SciencesBioquímica Vegetal y Biología MolecularDirección General de Enseñanza Superior e Investigación Científica (DGESIC). EspañaJunta de Andalucía1999info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfapplication/pdfhttps://hdl.handle.net/11441/69683https://doi.org/10.1073/pnas.96.13.7161reponame:idUS. Depósito de Investigación de la Universidad de Sevillainstname:Universidad de Sevilla (US)InglésProceedings of the National Academy of Sciences of the United States of America, 96 (13), 7161-7166.http://dx.doi.org/10.1073/pnas.96.13.7161info:eu-repo/semantics/openAccessoai:idus.us.es:11441/696832026-06-17T12:51:07Z
dc.title.none.fl_str_mv Glutamine synthetase inactivation by protein-protein interaction
title Glutamine synthetase inactivation by protein-protein interaction
spellingShingle Glutamine synthetase inactivation by protein-protein interaction
García-Dominguez, Mario
Cyanobacteria
Enzyme regulation
Nitrogen metabolism
Synechocystis 6803
title_short Glutamine synthetase inactivation by protein-protein interaction
title_full Glutamine synthetase inactivation by protein-protein interaction
title_fullStr Glutamine synthetase inactivation by protein-protein interaction
title_full_unstemmed Glutamine synthetase inactivation by protein-protein interaction
title_sort Glutamine synthetase inactivation by protein-protein interaction
dc.creator.none.fl_str_mv García-Dominguez, Mario
Reyes, José C.
Florencio Bellido, Francisco Javier
author García-Dominguez, Mario
author_facet García-Dominguez, Mario
Reyes, José C.
Florencio Bellido, Francisco Javier
author_role author
author2 Reyes, José C.
Florencio Bellido, Francisco Javier
author2_role author
author
dc.contributor.none.fl_str_mv Bioquímica Vegetal y Biología Molecular
Dirección General de Enseñanza Superior e Investigación Científica (DGESIC). España
Junta de Andalucía
dc.subject.none.fl_str_mv Cyanobacteria
Enzyme regulation
Nitrogen metabolism
Synechocystis 6803
topic Cyanobacteria
Enzyme regulation
Nitrogen metabolism
Synechocystis 6803
description Glutamine synthetase (GS; EC 6.3.1.2) is the pivotal enzyme of nitrogen metabolism in prokaryotes. Control of bacterial GS activity by reversible adenylylation has provided one of the classical paradigms of signal transduction by cyclic cascades. By contrast, in the present work we show that cyanobacterial GS is controlled by a different mechanism that involves the interaction of two inhibitory polypeptides with the enzyme. Both inactivating factors (IFs), named IF7 and IF17, are required in vivo for complete GS inactivation. Inactive GS-IF7 and GS-IF17 complexes were reconstituted in vitro by using Escherichia coli-expressed purified proteins. Our data suggest that control of GS activity is exerted by regulating the levels of IF7 and IF17.
publishDate 1999
dc.date.none.fl_str_mv 1999
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/11441/69683
https://doi.org/10.1073/pnas.96.13.7161
url https://hdl.handle.net/11441/69683
https://doi.org/10.1073/pnas.96.13.7161
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Proceedings of the National Academy of Sciences of the United States of America, 96 (13), 7161-7166.
http://dx.doi.org/10.1073/pnas.96.13.7161
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv National Academy of Sciences
publisher.none.fl_str_mv National Academy of Sciences
dc.source.none.fl_str_mv reponame:idUS. Depósito de Investigación de la Universidad de Sevilla
instname:Universidad de Sevilla (US)
instname_str Universidad de Sevilla (US)
reponame_str idUS. Depósito de Investigación de la Universidad de Sevilla
collection idUS. Depósito de Investigación de la Universidad de Sevilla
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15.300724

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