A coiled coil switch mediates cold sensing by the thermosensory protein DesK

Autores
Saita, Emilio Adolfo; Abriata, Luciano Andres; Tsai, Yi Ting; Trajtenberg, Felipe; Lemmin, Thomas; Buschiazzo, Alejandro; Dal Peraro, Matteo; de Mendoza, Diego; Albanesi, Daniela
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The thermosensor histidine kinase DesK from Bacillus subtilis senses changes in membrane fluidity initiating an adaptive response. Structural changes in DesK have been implicated in transmembrane signaling, but direct evidence is still lacking. On the basis of structure-guided mutagenesis, we now propose a mechanism of DesK-mediated signal sensing and transduction. The data indicate that stabilization/destabilization of a 2-helix coiled coil, which connects the transmembrane sensory domain of DesK to its cytosolic catalytic region, is crucial to control its signaling state. Computational modeling and simulations reveal couplings between protein, water and membrane mechanics. We propose that membrane thickening is the main driving force for signal sensing and that it acts by inducing helix stretching and rotation prompting an asymmetric kinase-competent state. Overall, the known structural changes of the sensor kinase, as well as further dynamic rearrangements that we now predict, consistently link structure determinants to activity modulation.
Fil: Saita, Emilio Adolfo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Abriata, Luciano Andres. Ecole Polytechnique Federale de Lausanne; Suiza. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Tsai, Yi Ting. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Trajtenberg, Felipe. Instituto Pasteur de Montevideo; Uruguay
Fil: Lemmin, Thomas. Ecole Polytechnique Federale de Lausanne; Suiza
Fil: Buschiazzo, Alejandro. Instituto Pasteur de Montevideo; Uruguay. Instituto Pasteur; Francia
Fil: Dal Peraro, Matteo. Ecole Polytechnique Federale de Lausanne; Suiza
Fil: de Mendoza, Diego. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Albanesi, Daniela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Materia
Desk
Histidine Kinase
Thermosensing
Transmembrane Signaling
2-Helix Coiled Coil
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/38134

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oai_identifier_str oai:ri.conicet.gov.ar:11336/38134
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling A coiled coil switch mediates cold sensing by the thermosensory protein DesKSaita, Emilio AdolfoAbriata, Luciano AndresTsai, Yi TingTrajtenberg, FelipeLemmin, ThomasBuschiazzo, AlejandroDal Peraro, Matteode Mendoza, DiegoAlbanesi, DanielaDeskHistidine KinaseThermosensingTransmembrane Signaling2-Helix Coiled Coilhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The thermosensor histidine kinase DesK from Bacillus subtilis senses changes in membrane fluidity initiating an adaptive response. Structural changes in DesK have been implicated in transmembrane signaling, but direct evidence is still lacking. On the basis of structure-guided mutagenesis, we now propose a mechanism of DesK-mediated signal sensing and transduction. The data indicate that stabilization/destabilization of a 2-helix coiled coil, which connects the transmembrane sensory domain of DesK to its cytosolic catalytic region, is crucial to control its signaling state. Computational modeling and simulations reveal couplings between protein, water and membrane mechanics. We propose that membrane thickening is the main driving force for signal sensing and that it acts by inducing helix stretching and rotation prompting an asymmetric kinase-competent state. Overall, the known structural changes of the sensor kinase, as well as further dynamic rearrangements that we now predict, consistently link structure determinants to activity modulation.Fil: Saita, Emilio Adolfo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Abriata, Luciano Andres. Ecole Polytechnique Federale de Lausanne; Suiza. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Tsai, Yi Ting. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Trajtenberg, Felipe. Instituto Pasteur de Montevideo; UruguayFil: Lemmin, Thomas. Ecole Polytechnique Federale de Lausanne; SuizaFil: Buschiazzo, Alejandro. Instituto Pasteur de Montevideo; Uruguay. Instituto Pasteur; FranciaFil: Dal Peraro, Matteo. Ecole Polytechnique Federale de Lausanne; SuizaFil: de Mendoza, Diego. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Albanesi, Daniela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaWiley Blackwell Publishing, Inc2015-10info: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/11336/38134Saita, Emilio Adolfo; Abriata, Luciano Andres; Tsai, Yi Ting; Trajtenberg, Felipe; Lemmin, Thomas; et al.; A coiled coil switch mediates cold sensing by the thermosensory protein DesK; Wiley Blackwell Publishing, Inc; Molecular Microbiology; 98; 2; 10-2015; 258-2710950-382XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1111/mmi.13118info:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1111/mmi.13118/abstractinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:10:00Zoai:ri.conicet.gov.ar:11336/38134instacron: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:34982025-09-03 10:10:01.256CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv A coiled coil switch mediates cold sensing by the thermosensory protein DesK
title A coiled coil switch mediates cold sensing by the thermosensory protein DesK
spellingShingle A coiled coil switch mediates cold sensing by the thermosensory protein DesK
Saita, Emilio Adolfo
Desk
Histidine Kinase
Thermosensing
Transmembrane Signaling
2-Helix Coiled Coil
title_short A coiled coil switch mediates cold sensing by the thermosensory protein DesK
title_full A coiled coil switch mediates cold sensing by the thermosensory protein DesK
title_fullStr A coiled coil switch mediates cold sensing by the thermosensory protein DesK
title_full_unstemmed A coiled coil switch mediates cold sensing by the thermosensory protein DesK
title_sort A coiled coil switch mediates cold sensing by the thermosensory protein DesK
dc.creator.none.fl_str_mv Saita, Emilio Adolfo
Abriata, Luciano Andres
Tsai, Yi Ting
Trajtenberg, Felipe
Lemmin, Thomas
Buschiazzo, Alejandro
Dal Peraro, Matteo
de Mendoza, Diego
Albanesi, Daniela
author Saita, Emilio Adolfo
author_facet Saita, Emilio Adolfo
Abriata, Luciano Andres
Tsai, Yi Ting
Trajtenberg, Felipe
Lemmin, Thomas
Buschiazzo, Alejandro
Dal Peraro, Matteo
de Mendoza, Diego
Albanesi, Daniela
author_role author
author2 Abriata, Luciano Andres
Tsai, Yi Ting
Trajtenberg, Felipe
Lemmin, Thomas
Buschiazzo, Alejandro
Dal Peraro, Matteo
de Mendoza, Diego
Albanesi, Daniela
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Desk
Histidine Kinase
Thermosensing
Transmembrane Signaling
2-Helix Coiled Coil
topic Desk
Histidine Kinase
Thermosensing
Transmembrane Signaling
2-Helix Coiled Coil
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The thermosensor histidine kinase DesK from Bacillus subtilis senses changes in membrane fluidity initiating an adaptive response. Structural changes in DesK have been implicated in transmembrane signaling, but direct evidence is still lacking. On the basis of structure-guided mutagenesis, we now propose a mechanism of DesK-mediated signal sensing and transduction. The data indicate that stabilization/destabilization of a 2-helix coiled coil, which connects the transmembrane sensory domain of DesK to its cytosolic catalytic region, is crucial to control its signaling state. Computational modeling and simulations reveal couplings between protein, water and membrane mechanics. We propose that membrane thickening is the main driving force for signal sensing and that it acts by inducing helix stretching and rotation prompting an asymmetric kinase-competent state. Overall, the known structural changes of the sensor kinase, as well as further dynamic rearrangements that we now predict, consistently link structure determinants to activity modulation.
Fil: Saita, Emilio Adolfo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Abriata, Luciano Andres. Ecole Polytechnique Federale de Lausanne; Suiza. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Tsai, Yi Ting. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Trajtenberg, Felipe. Instituto Pasteur de Montevideo; Uruguay
Fil: Lemmin, Thomas. Ecole Polytechnique Federale de Lausanne; Suiza
Fil: Buschiazzo, Alejandro. Instituto Pasteur de Montevideo; Uruguay. Instituto Pasteur; Francia
Fil: Dal Peraro, Matteo. Ecole Polytechnique Federale de Lausanne; Suiza
Fil: de Mendoza, Diego. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Albanesi, Daniela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
description The thermosensor histidine kinase DesK from Bacillus subtilis senses changes in membrane fluidity initiating an adaptive response. Structural changes in DesK have been implicated in transmembrane signaling, but direct evidence is still lacking. On the basis of structure-guided mutagenesis, we now propose a mechanism of DesK-mediated signal sensing and transduction. The data indicate that stabilization/destabilization of a 2-helix coiled coil, which connects the transmembrane sensory domain of DesK to its cytosolic catalytic region, is crucial to control its signaling state. Computational modeling and simulations reveal couplings between protein, water and membrane mechanics. We propose that membrane thickening is the main driving force for signal sensing and that it acts by inducing helix stretching and rotation prompting an asymmetric kinase-competent state. Overall, the known structural changes of the sensor kinase, as well as further dynamic rearrangements that we now predict, consistently link structure determinants to activity modulation.
publishDate 2015
dc.date.none.fl_str_mv 2015-10
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/11336/38134
Saita, Emilio Adolfo; Abriata, Luciano Andres; Tsai, Yi Ting; Trajtenberg, Felipe; Lemmin, Thomas; et al.; A coiled coil switch mediates cold sensing by the thermosensory protein DesK; Wiley Blackwell Publishing, Inc; Molecular Microbiology; 98; 2; 10-2015; 258-271
0950-382X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/38134
identifier_str_mv Saita, Emilio Adolfo; Abriata, Luciano Andres; Tsai, Yi Ting; Trajtenberg, Felipe; Lemmin, Thomas; et al.; A coiled coil switch mediates cold sensing by the thermosensory protein DesK; Wiley Blackwell Publishing, Inc; Molecular Microbiology; 98; 2; 10-2015; 258-271
0950-382X
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1111/mmi.13118
info:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1111/mmi.13118/abstract
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Wiley Blackwell Publishing, Inc
publisher.none.fl_str_mv Wiley Blackwell Publishing, Inc
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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