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

Vista sencilla de ítem
dc.citation.titleMolecular Microbiology
dc.citation.volume98
dc.creatorSaita, Emilio Adolfo
dc.creatorAbriata, Luciano Andrés
dc.creatorTsai, Yi-Ting
dc.creatorTrajtenberg, Felipe
dc.creatorLemmin, Thomas
dc.creatorBuschiazzo, Alejandro
dc.creatorDal Peraro, Matteo
dc.creatorDe Mendoza, Diego
dc.creatorAlbanesi, Daniela
dc.date.accessioned2024-06-13T14:03:33Z
dc.date.available2024-06-13T14:03:33Z
dc.date.issued2015-10-08
dc.description.abstractThe 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.
dc.description.filFil: Saita, Emilio Adolfo. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario (IBR-CONICET). Laboratorio de Fisiología Microbiana; Argentina.
dc.description.filFil: Abriata, Luciano Andrés. École Polytechnique Fédérale de Lausanne (EPFL). School of Life Sciences. Laboratory for Biomolecular Modeling; Switzerland.
dc.description.filFil: Abriata, Luciano Andrés. Swiss Institute of Bioinformatics (SIB); Switzerland.
dc.description.filFil: Tsai, Yi-Ting. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario (IBR-CONICET). Laboratorio de Fisiología Microbiana; Argentina.
dc.description.filFil: Trajtenberg, Felipe. Institut Pasteur de Montevideo. Unidad de Cristalografía de Proteínas; Uruguay.
dc.description.filFil: Lemmin, Thomas. École Polytechnique Fédérale de Lausanne (EPFL). School of Life Sciences. Laboratory for Biomolecular Modeling; Switzerland.
dc.description.filFil: Lemmin, Thomas. Swiss Institute of Bioinformatics (SIB); Switzerland.
dc.description.filFil: Buschiazzo, Alejandro. Institut Pasteur de Montevideo. Unidad de Cristalografía de Proteínas; Uruguay.
dc.description.filFil: Buschiazzo, Alejandro. Institut Pasteur. Département de Biologie Structurale et Chimie; France.
dc.description.filFil: Dal Peraro, Matteo. École Polytechnique Fédérale de Lausanne (EPFL). School of Life Sciences. Laboratory for Biomolecular Modeling; Switzerland.
dc.description.filFil: Dal Peraro, Matteo. Swiss Institute of Bioinformatics (SIB); Switzerland.
dc.description.filFil: De Mendoza, Diego. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario (IBR-CONICET). Laboratorio de Fisiología Microbiana; Argentina.
dc.description.filFil: Albanesi, Daniela. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario (IBR-CONICET). Laboratorio de Fisiología Microbiana; Argentina.
dc.description.sponsorshipConsejo Nacional de Investigaciones Científicas y Técnicas (CONICET)
dc.description.sponsorshipAgencia Nacional de Promoción de la Investigación, el Desarrollo Tecnológico y la Innovación (Agencia I+D+i)
dc.description.sponsorshipSwiss National Science Foundation (SNSF)
dc.description.sponsorshipEuropean Molecular Biology Organization (EMBO)
dc.description.sponsorshipMarie Sklodowska-Curie Actions (MSCA)
dc.description.versionpeerreviewed
dc.format.extent1-14
dc.identifier.e-issn1365-2958
dc.identifier.issn0950-382X
dc.identifier.urihttps://hdl.handle.net/2133/27300
dc.language.isoen
dc.publisherWiley
dc.relation.publisherversionhttps://doi.org/10.1111/mmi.13118
dc.relation.publisherversionhttps://onlinelibrary.wiley.com/doi/10.1111/mmi.13118
dc.rightsopenAccess
dc.rights.holderSaita, Emilio Adolfo
dc.rights.holderAbriata, Luciano Andrés
dc.rights.holderTsai, Yi-Ting
dc.rights.holderTrajtenberg, Felipe
dc.rights.holderLemmin, Thomas
dc.rights.holderBuschiazzo, Alejandro
dc.rights.holderDal Peraro, Matteo
dc.rights.holderDe Mendoza, Diego
dc.rights.holderAlbanesi, Daniela
dc.rights.holderUniversidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas
dc.rights.textAttribution-NonCommercial-NoDerivs 4.0 International
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subjectDesK
dc.subjectHistidine kinase
dc.subjectThermosensor
dc.subjectMembrane fluidity
dc.subjectBacillus subtilis
dc.titleA coiled coil switch mediates cold sensing by the thermosensory protein DesK
dc.typearticulo
dc.type.collectionarticulo
dc.type.versionpublishedVersion

Archivos

Bloque original
Mostrando 1 - 1 de 1
Miniatura
Nombre:
File - Molecular Microbiology - 2015 - Saita - A coiled coil [...].pdf
Tamaño:
6.15 MB
Formato:
Adobe Portable Document Format
Descargar
Bloque de licencias
Mostrando 1 - 1 de 1
Nombre:
license.txt
Tamaño:
3.87 KB
Formato:
Item-specific license agreed upon to submission
Descripción:
Descargar

Colecciones

(FBIOyF) Departamento de Química Orgánica - Artículos
(FBIOyF) Departamento de Microbiología - Artículos