Argentina
| info:eu-repo/semantics/article
Interhelical h-bonds modulate the activity of a polytopic transmembrane kinase
dc.creator | Almada, Juan Cruz | |
dc.creator | Bortolotti, Ana | |
dc.creator | Ruysschaert, Jean Marie | |
dc.creator | de Mendoza, Diego | |
dc.creator | Inda, María Eugenia | |
dc.creator | Cybulski, Larisa Estefania | |
dc.date.accessioned | 2022-03-17T03:56:10Z | |
dc.date.accessioned | 2022-10-15T08:08:09Z | |
dc.date.available | 2022-03-17T03:56:10Z | |
dc.date.available | 2022-10-15T08:08:09Z | |
dc.date.created | 2022-03-17T03:56:10Z | |
dc.date.issued | 2021-07 | |
dc.identifier | Almada, Juan Cruz; Bortolotti, Ana; Ruysschaert, Jean Marie; de Mendoza, Diego; Inda, María Eugenia; et al.; Interhelical h-bonds modulate the activity of a polytopic transmembrane kinase; Multidisciplinary Digital Publishing Institute; Biomolecules; 11; 7; 7-2021; 1-12 | |
dc.identifier | 2218-273X | |
dc.identifier | http://hdl.handle.net/11336/153484 | |
dc.identifier | 2218-273X | |
dc.identifier | CONICET Digital | |
dc.identifier | CONICET | |
dc.identifier.uri | https://repositorioslatinoamericanos.uchile.cl/handle/2250/4363583 | |
dc.description.abstract | DesK 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. | |
dc.language | eng | |
dc.publisher | Multidisciplinary Digital Publishing Institute | |
dc.relation | info:eu-repo/semantics/altIdentifier/doi/https://www.mdpi.com/2218-273X/11/7/938 | |
dc.relation | info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.3390/biom11070938 | |
dc.rights | https://creativecommons.org/licenses/by/2.5/ar/ | |
dc.rights | info:eu-repo/semantics/openAccess | |
dc.subject | DIMERISATION MOTIF | |
dc.subject | HISTIDINE KINASE | |
dc.subject | HYDROGEN BOND INTERACTION | |
dc.subject | RECEPTOR | |
dc.subject | SIGNAL TRANSDUCTION | |
dc.subject | TRANSMEMBRANE PROTEIN INTERACTIONS | |
dc.title | Interhelical h-bonds modulate the activity of a polytopic transmembrane kinase | |
dc.type | info:eu-repo/semantics/article | |
dc.type | info:ar-repo/semantics/artículo | |
dc.type | info:eu-repo/semantics/publishedVersion |