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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/38134
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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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13.13397 |