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Interhelical h-bonds modulate the activity of a polytopic transmembrane kinase

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dc.citation.titleBiomoleculeses
dc.citation.volume11
dc.creatorAlmada, Juan Cruz
dc.creatorBortolotti, Ana
dc.creatorRuysschaert, Jane Marie
dc.creatorDe Mendoza, Diego
dc.creatorCybulski, Larisa Estefanía
dc.date.accessioned2022-03-28T20:08:23Z
dc.date.available2022-03-28T20:08:23Z
dc.date.issued2021
dc.descriptionDesK is a Histidine Kinase that allows Bacillus subtilis to maintain lipid homeostasis in response to changes in the environment. It is located in the membrane, and has five transmembrane helices and a cytoplasmic catalytic domain. The transmembrane region triggers the phosphorylation of the catalytic domain as soon as the membrane lipids rigidify. In this research, we study how transmembrane inter-helical interactions contribute to signal transmission; we designed a coexpression system that allows studying in vivo interactions between transmembrane helices. By Alanine-replacements, we identified a group of polar uncharged residues, whose side chains contain hydrogen-bond donors or acceptors, which are required for the interaction with other DesK transmembrane helices; a particular array of H-bond- residues plays a key role in signaling, transmitting information detected at the membrane level into the cell to finally trigger an adaptive response.es
dc.description.filFil: Almada, Juan Cruz. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología. Argentina.es
dc.description.filFil: Bortolotti, Ana. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología. Argentina.es
dc.description.filFil: Ruysschaert, Jean Marie. Université Libre de Bruxelles. Center for Structural Biology and Bioinformatics. Laboratory for the Structure and Function of Biological Membranes. Belgium.es
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.es
dc.description.filFil: Inda, María Eugenia. Massachusetts Institute of Technology. Department of Electrical Engineering and Computer Science. Research Laboratory of Electronics. Cambridge.es
dc.description.filFil: Inda, María Eugenia. Massachusetts Institute of Technology. MIT Synthetic Biology Center. Cambridge.es
dc.description.filFil:Cybulski, Larisa Estefanía. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología. Argentina.es
dc.description.sponsorshipConsejo Nacional de Investigaciones Científicas y Técnicas (CONICET): PIP 2015-0905
dc.description.sponsorshipMinisterio de Ciencia, Tecnología e Innovación Productiva (MINCyT)
dc.description.sponsorshipAgencia Nacional de Promoción Científica y Tecnológica (ANPCyT)
dc.description.sponsorshipFondo para la Investigación Científica y Tecnológica (FonCyT): PICT 2017-0488
dc.formatapplication/pdf
dc.format.extent1-12es
dc.identifier.issn2218-273Xes
dc.identifier.urihttp://hdl.handle.net/2133/23273
dc.language.isoenges
dc.publisherMDPIes
dc.relation.publisherversionhttps://www.mdpi.com/2218-273X/11/7/938es
dc.relation.publisherversionhttps://doi.org/10.3390/biom11070938
dc.rightsopenAccesses
dc.rights.holderAlmada, Juan Cruzes
dc.rights.holderBortolotti, Anaes
dc.rights.holderRuysschaert, Jean Mariees
dc.rights.holderDe Mendoza, Diegoes
dc.rights.holderInda, María Eugeniaes
dc.rights.holderCybulski, Larisa Estefaníaes
dc.rights.textAttribution 4.0 International (CC BY 4.0)es
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/*
dc.subjectTransmembrane Protein Interactionses
dc.subjectHydrogen Bond Interactiones
dc.subjectSignal Transductiones
dc.subjectHistidine Kinasees
dc.subjectDimerisation Motifes
dc.subjectReceptores
dc.titleInterhelical h-bonds modulate the activity of a polytopic transmembrane kinasees
dc.typepublishedVersion
dc.typearticle
dc.typeartículo
dc.type.collectionarticulo
dc.type.versionpublishedVersion

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(FBIOyF) Departamento de Química Física - Artículo de Revista