Identification of the repressor subdomain within the signal reception module of the prokaryotic enhancer-binding protein XyIR of Pseudomonas putida

In the presence of m-xylene, the protein XyIR encoded by the TOL plasmid of Pseudomonas putida, activates the σ54-dependent promoter Pu. Early activation stages involve the release of the intramolecular repression caused by the signal reception N-terminal (A domain) of XyIR, on the central module of...

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Autores: Pérez-Martín, José, Lorenzo, Víctor de
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:1996
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/340786
Acceso en línea:http://hdl.handle.net/10261/340786
Access Level:acceso abierto
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spelling Identification of the repressor subdomain within the signal reception module of the prokaryotic enhancer-binding protein XyIR of Pseudomonas putidaPérez-Martín, JoséLorenzo, Víctor deIn the presence of m-xylene, the protein XyIR encoded by the TOL plasmid of Pseudomonas putida, activates the σ54-dependent promoter Pu. Early activation stages involve the release of the intramolecular repression caused by the signal reception N-terminal (A domain) of XyIR, on the central module of the protein. A genetic approach has been followed to locate the specific segment within A domain of XyIR that is directly responsible for its down-regulation in the absence of inducer, as compared to that involved in effector (m-xylene) binding. For this, a reporter Escherichia coli strain carrying a monocopy transcriptional fusion of Pu to lacZ was transformed with a collection of plasmids encoding equivalent truncated varieties of XyIR, consisting of nested and internal deletions throughout the entire A domain. Examination of the resulting phenotypes allowed the assignment of the A domain region near the central activation domain, as the portion of the protein responsible for the specific repression of XyIR activity in the absence of m-xylene.This work was supported by Grant BIO95– 0788 of the Spanish Comisio´n Interministerial de Ciencia y Tecnologı´a (CICYT) and Contract BIOTECH BIO2-CT92– 0084 of the European Union. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this factAmerican Society for Biochemistry and Molecular BiologyElsevierComisión Interministerial de Ciencia y Tecnología, CICYT (España)European CommissionConsejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]2023202319962023info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionapplication/pdfhttp://hdl.handle.net/10261/340786reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttp://dx.doi.org/10.1074/jbc.271.14.7899Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/3407862026-05-22T06:33:51Z
dc.title.none.fl_str_mv Identification of the repressor subdomain within the signal reception module of the prokaryotic enhancer-binding protein XyIR of Pseudomonas putida
title Identification of the repressor subdomain within the signal reception module of the prokaryotic enhancer-binding protein XyIR of Pseudomonas putida
spellingShingle Identification of the repressor subdomain within the signal reception module of the prokaryotic enhancer-binding protein XyIR of Pseudomonas putida
Pérez-Martín, José
title_short Identification of the repressor subdomain within the signal reception module of the prokaryotic enhancer-binding protein XyIR of Pseudomonas putida
title_full Identification of the repressor subdomain within the signal reception module of the prokaryotic enhancer-binding protein XyIR of Pseudomonas putida
title_fullStr Identification of the repressor subdomain within the signal reception module of the prokaryotic enhancer-binding protein XyIR of Pseudomonas putida
title_full_unstemmed Identification of the repressor subdomain within the signal reception module of the prokaryotic enhancer-binding protein XyIR of Pseudomonas putida
title_sort Identification of the repressor subdomain within the signal reception module of the prokaryotic enhancer-binding protein XyIR of Pseudomonas putida
dc.creator.none.fl_str_mv Pérez-Martín, José
Lorenzo, Víctor de
author Pérez-Martín, José
author_facet Pérez-Martín, José
Lorenzo, Víctor de
author_role author
author2 Lorenzo, Víctor de
author2_role author
dc.contributor.none.fl_str_mv Comisión Interministerial de Ciencia y Tecnología, CICYT (España)
European Commission
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
description In the presence of m-xylene, the protein XyIR encoded by the TOL plasmid of Pseudomonas putida, activates the σ54-dependent promoter Pu. Early activation stages involve the release of the intramolecular repression caused by the signal reception N-terminal (A domain) of XyIR, on the central module of the protein. A genetic approach has been followed to locate the specific segment within A domain of XyIR that is directly responsible for its down-regulation in the absence of inducer, as compared to that involved in effector (m-xylene) binding. For this, a reporter Escherichia coli strain carrying a monocopy transcriptional fusion of Pu to lacZ was transformed with a collection of plasmids encoding equivalent truncated varieties of XyIR, consisting of nested and internal deletions throughout the entire A domain. Examination of the resulting phenotypes allowed the assignment of the A domain region near the central activation domain, as the portion of the protein responsible for the specific repression of XyIR activity in the absence of m-xylene.
publishDate 1996
dc.date.none.fl_str_mv 1996
2023
2023
2023
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/10261/340786
url http://hdl.handle.net/10261/340786
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv http://dx.doi.org/10.1074/jbc.271.14.7899
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv American Society for Biochemistry and Molecular Biology
Elsevier
publisher.none.fl_str_mv American Society for Biochemistry and Molecular Biology
Elsevier
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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score 15,811543

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