Transmembrane prolines mediate signal sensing and decoding in Bacillus subtilis DesK histidine kinase

Vista sencilla de ítem
dc.citation.titlemBio
dc.citation.volume10(6)
dc.citation.volume10(6)
dc.creatorFernández, Pilar
dc.creatorPorrini, Lucía
dc.creatorAlbanesi, Daniela
dc.creatorAbriata, Luciano Andrés
dc.creatorDal Peraro, Matteo
dc.creatorDe Mendoza, Diego
dc.creatorMansilla, María Cecilia
dc.date.accessioned2021-03-11T18:41:43Z
dc.date.available2021-03-11T18:41:43Z
dc.date.issued2019-11-26
dc.descriptionEnvironmental awareness is an essential attribute of all organisms. The homeoviscous adaptation system of Bacillus subtilis provides a powerful experimen tal model for the investigation of stimulus detection and signaling mechanisms at the molecular level. These bacteria sense the order of membrane lipids with the transmembrane (TM) protein DesK, which has an N-terminal sensor domain and an intracellular catalytic effector domain. DesK exhibits autokinase activity as well as phosphotransferase and phosphatase activities toward a cognate response regulator, DesR, that controls the expression of an enzyme that remodels membrane fluidity when the temperature drops below 30°C. Membrane fluidity signals are transmit ted from the DesK sensor domain to the effector domain via rotational movements of a connecting 2-helix coiled coil (2-HCC). Previous molecular dynamic simulations suggested important roles for TM prolines in transducing the initial signals of mem brane fluidity status to the 2-HCC. Here, we report that individual replacement of prolines in DesKs TM1 and TM5 helices by alanine (DesKPA) locked DesK in a phosphatase-ON state, abrogating membrane fluidity responses. An unbiased muta genic screen identified the L174P replacement in the internal side of the repeated heptad of the 2-HCC structure that alleviated the signaling defects of every trans membrane DesKPA substitution. Moreover, substitutions by proline in other internal positions of the 2-HCC reestablished the kinase-ON state of the DesKPA mutants. These results imply that TM prolines are essential for finely tuned signal generation by the N-terminal sensor helices, facilitating a conformational control by the meta stable 2-HCC domain of the DesK signaling state.es
dc.description.filFil: Fernández, Pilar. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario (IBR - CONICET); Argentina.
dc.description.filFil: Porrini, Lucía. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario (IBR - CONICET); Argentina.
dc.description.filFil: Porrini, Lucía. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología; 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); Argentina.
dc.description.filFil: Albanesi, Daniela. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología; Argentina.
dc.description.filFil: Abriata, Luciano A. École Polytechnique Fédérale de Lausanne. Institute of Bioengineering; Switzerland.
dc.description.filFil: Abriata, Luciano A. Swiss Institute of Bioinformatics; Switzerland.
dc.description.filFil: Dal Peraro, Matteo. École Polytechnique Fédérale de Lausanne. Institute of Bioengineering; Switzerland.
dc.description.filFil: Dal Peraro, Matteo. Swiss Institute of Bioinformatics; 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); Argentina.
dc.description.filFil: De Mendoza, Diego. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología; Argentina.
dc.description.filFil: De Mendoza, Diego. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología; Argentina.
dc.description.filFil: Mansilla, María C. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario (IBR - CONICET); Argentina.
dc.description.filFil: Mansilla, María C. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología; Argentina.
dc.description.sponsorshipAgencia Nacional de Promoción Científica y Tecnológica (ANPCyT): PICT 2010-2678 y PID 2013-0043es
dc.description.sponsorshipSwiss National Science Foundationes
dc.formatapplication/pdf
dc.format.extent1-15
dc.identifier.issn2150-7511
dc.identifier.urihttp://hdl.handle.net/2133/20127
dc.language.isoenges
dc.publisherAmerican Society for Microbiologyes
dc.relation.publisherversionhttps://doi.org/10.1128/mbio.02564-19es
dc.relation.publisherversionhttps://mbio.asm.org/content/10/6/e02564-19es
dc.rightsopenAccesses
dc.rights.holderUniversidad Nacional de Rosarioes
dc.rights.holderFernández, Pilares
dc.rights.holderPorrini, Lucíaes
dc.rights.holderAlbanesi, Danielaes
dc.rights.holderAbriata, Luciano A.es
dc.rights.holderDal Peraro, Matteoes
dc.rights.holderDe Mendoza, Diegoes
dc.rights.holderMansilla, María C.es
dc.rights.textAttribution 4.0 International (CC BY 4.0)es
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/*
dc.subjectHistidine Kinasees
dc.subjectProlinees
dc.subjectThermosensinges
dc.subjectTwo-component Regulatory Systemses
dc.titleTransmembrane prolines mediate signal sensing and decoding in Bacillus subtilis DesK histidine kinasees
dc.typepublishedVersion

Archivos

Bloque original
Mostrando 1 - 1 de 1
Miniatura
Nombre:
25 mBio-2019-Fernández-e02564-19.full.pdf
Tamaño:
2.22 MB
Formato:
Adobe Portable Document Format
Descripción:
versión post-print
Descargar
Bloque de licencias
Mostrando 1 - 1 de 1
Nombre:
license.txt
Tamaño:
3.59 KB
Formato:
Item-specific license agreed upon to submission
Descripción:
Descargar

Colecciones

(FBIOyF) Departamento de Microbiología - Artículos