A chemoreceptor from Pseudomonas putida forms active signaling complexes in Escherichia coli

Autores
Herrera Seitz, Karina; Soto, Débora; Studdert, Claudia Alicia
Año de publicación
2012
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Chemoreceptors sense environmental stimuli and transmit the information to the flagellar motors via a histidine kinase that controls the phosphorylation level of the effector protein CheY. The cytoplasmic domain of chemoreceptors consists of a long a-helical hairpin that forms, in the dimer, a coiled-coil four-helix bundle. Even though the sequence and general structure of the cytoplasmic domain are strongly conserved within Eubacteria and Archaea, the total length of the a-helical hairpin is variable and defines seven classes of chemoreceptors. In this work we assessed the functional properties of a Pseudomonas receptor when assembled in signalling complexes with Escherichia coli proteins. Our results show that the foreign receptor does not confer fully chemotactic abilities upon E. coli cells, but is able to form active ternary complexes that respond to the specific stimuli by modulating the activity of the associated kinase. The observed responses are subject to adaptation, depending on the presence of the methylation enzymes CheR and/or CheB. The ability of foreign receptors to signal through signalling complexes with non-cognate proteins would allow the use of the well-studied E. coli system to reveal the detection specificity of uncharacterized chemoreceptors from other micro-organisms.
Fil: Herrera Seitz, Karina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina
Fil: Soto, Débora. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina
Fil: Studdert, Claudia Alicia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina
Materia
CHEMORECEPTORS
CHEMOTAXIS
PSEUDOMONAS PUTIDA
BACTERIA
ESCHERICHIA COLI
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/235890
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/235890
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling A chemoreceptor from Pseudomonas putida forms active signaling complexes in Escherichia coliHerrera Seitz, KarinaSoto, DéboraStuddert, Claudia AliciaCHEMORECEPTORSCHEMOTAXISPSEUDOMONAS PUTIDABACTERIAESCHERICHIA COLIhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Chemoreceptors sense environmental stimuli and transmit the information to the flagellar motors via a histidine kinase that controls the phosphorylation level of the effector protein CheY. The cytoplasmic domain of chemoreceptors consists of a long a-helical hairpin that forms, in the dimer, a coiled-coil four-helix bundle. Even though the sequence and general structure of the cytoplasmic domain are strongly conserved within Eubacteria and Archaea, the total length of the a-helical hairpin is variable and defines seven classes of chemoreceptors. In this work we assessed the functional properties of a Pseudomonas receptor when assembled in signalling complexes with Escherichia coli proteins. Our results show that the foreign receptor does not confer fully chemotactic abilities upon E. coli cells, but is able to form active ternary complexes that respond to the specific stimuli by modulating the activity of the associated kinase. The observed responses are subject to adaptation, depending on the presence of the methylation enzymes CheR and/or CheB. The ability of foreign receptors to signal through signalling complexes with non-cognate proteins would allow the use of the well-studied E. coli system to reveal the detection specificity of uncharacterized chemoreceptors from other micro-organisms.Fil: Herrera Seitz, Karina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; ArgentinaFil: Soto, Débora. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; ArgentinaFil: Studdert, Claudia Alicia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; ArgentinaSociety for General Microbiology2012-06-22info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/235890Herrera Seitz, Karina; Soto, Débora; Studdert, Claudia Alicia; A chemoreceptor from Pseudomonas putida forms active signaling complexes in Escherichia coli; Society for General Microbiology; Microbiology-UK; 158; 9; 22-6-2012; 2283-22922516-8290CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.microbiologyresearch.org/content/journal/micro/10.1099/mic.0.059899-0info:eu-repo/semantics/altIdentifier/doi/10.1099/mic.0.059899-0info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-10T13:02:37Zoai:ri.conicet.gov.ar:11336/235890instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-10 13:02:37.845CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv A chemoreceptor from Pseudomonas putida forms active signaling complexes in Escherichia coli
title A chemoreceptor from Pseudomonas putida forms active signaling complexes in Escherichia coli
spellingShingle A chemoreceptor from Pseudomonas putida forms active signaling complexes in Escherichia coli
Herrera Seitz, Karina
CHEMORECEPTORS
CHEMOTAXIS
PSEUDOMONAS PUTIDA
BACTERIA
ESCHERICHIA COLI
title_short A chemoreceptor from Pseudomonas putida forms active signaling complexes in Escherichia coli
title_full A chemoreceptor from Pseudomonas putida forms active signaling complexes in Escherichia coli
title_fullStr A chemoreceptor from Pseudomonas putida forms active signaling complexes in Escherichia coli
title_full_unstemmed A chemoreceptor from Pseudomonas putida forms active signaling complexes in Escherichia coli
title_sort A chemoreceptor from Pseudomonas putida forms active signaling complexes in Escherichia coli
dc.creator.none.fl_str_mv Herrera Seitz, Karina
Soto, Débora
Studdert, Claudia Alicia
author Herrera Seitz, Karina
author_facet Herrera Seitz, Karina
Soto, Débora
Studdert, Claudia Alicia
author_role author
author2 Soto, Débora
Studdert, Claudia Alicia
author2_role author
author
dc.subject.none.fl_str_mv CHEMORECEPTORS
CHEMOTAXIS
PSEUDOMONAS PUTIDA
BACTERIA
ESCHERICHIA COLI
topic CHEMORECEPTORS
CHEMOTAXIS
PSEUDOMONAS PUTIDA
BACTERIA
ESCHERICHIA COLI
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Chemoreceptors sense environmental stimuli and transmit the information to the flagellar motors via a histidine kinase that controls the phosphorylation level of the effector protein CheY. The cytoplasmic domain of chemoreceptors consists of a long a-helical hairpin that forms, in the dimer, a coiled-coil four-helix bundle. Even though the sequence and general structure of the cytoplasmic domain are strongly conserved within Eubacteria and Archaea, the total length of the a-helical hairpin is variable and defines seven classes of chemoreceptors. In this work we assessed the functional properties of a Pseudomonas receptor when assembled in signalling complexes with Escherichia coli proteins. Our results show that the foreign receptor does not confer fully chemotactic abilities upon E. coli cells, but is able to form active ternary complexes that respond to the specific stimuli by modulating the activity of the associated kinase. The observed responses are subject to adaptation, depending on the presence of the methylation enzymes CheR and/or CheB. The ability of foreign receptors to signal through signalling complexes with non-cognate proteins would allow the use of the well-studied E. coli system to reveal the detection specificity of uncharacterized chemoreceptors from other micro-organisms.
Fil: Herrera Seitz, Karina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina
Fil: Soto, Débora. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina
Fil: Studdert, Claudia Alicia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina
description Chemoreceptors sense environmental stimuli and transmit the information to the flagellar motors via a histidine kinase that controls the phosphorylation level of the effector protein CheY. The cytoplasmic domain of chemoreceptors consists of a long a-helical hairpin that forms, in the dimer, a coiled-coil four-helix bundle. Even though the sequence and general structure of the cytoplasmic domain are strongly conserved within Eubacteria and Archaea, the total length of the a-helical hairpin is variable and defines seven classes of chemoreceptors. In this work we assessed the functional properties of a Pseudomonas receptor when assembled in signalling complexes with Escherichia coli proteins. Our results show that the foreign receptor does not confer fully chemotactic abilities upon E. coli cells, but is able to form active ternary complexes that respond to the specific stimuli by modulating the activity of the associated kinase. The observed responses are subject to adaptation, depending on the presence of the methylation enzymes CheR and/or CheB. The ability of foreign receptors to signal through signalling complexes with non-cognate proteins would allow the use of the well-studied E. coli system to reveal the detection specificity of uncharacterized chemoreceptors from other micro-organisms.
publishDate 2012
dc.date.none.fl_str_mv 2012-06-22
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/235890
Herrera Seitz, Karina; Soto, Débora; Studdert, Claudia Alicia; A chemoreceptor from Pseudomonas putida forms active signaling complexes in Escherichia coli; Society for General Microbiology; Microbiology-UK; 158; 9; 22-6-2012; 2283-2292
2516-8290
CONICET Digital
CONICET
url http://hdl.handle.net/11336/235890
identifier_str_mv Herrera Seitz, Karina; Soto, Débora; Studdert, Claudia Alicia; A chemoreceptor from Pseudomonas putida forms active signaling complexes in Escherichia coli; Society for General Microbiology; Microbiology-UK; 158; 9; 22-6-2012; 2283-2292
2516-8290
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.microbiologyresearch.org/content/journal/micro/10.1099/mic.0.059899-0
info:eu-repo/semantics/altIdentifier/doi/10.1099/mic.0.059899-0
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Society for General Microbiology
publisher.none.fl_str_mv Society for General Microbiology
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 12.993085

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