| dc.creator | Almada, Juan Cruz | |
| dc.creator | Bortolotti, Ana | |
| dc.creator | Ruysschaert, Jane Marie | |
| dc.creator | De Mendoza, Diego | |
| dc.creator | Cybulski, Larisa Estefanía | |
| dc.date | 2022-03-28T20:08:23Z | |
| dc.date | 2022-03-28T20:08:23Z | |
| dc.date | 2021 | |
| dc.date | 2022-03-28T20:08:23Z | |
| dc.date | 2022-03-28T20:08:23Z | |
| dc.date | 2021 | |
| dc.identifier | 2218-273X | |
| dc.identifier | http://hdl.handle.net/2133/23273 | |
| dc.identifier | http://hdl.handle.net/2133/23273 | |
| dc.description | 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.description | Fil: Almada, Juan Cruz. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología. Argentina. | |
| dc.description | Fil: Bortolotti, Ana. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología. Argentina. | |
| dc.description | Fil: Ruysschaert, Jean Marie. Université Libre de Bruxelles. Center for Structural Biology and Bioinformatics. Laboratory for the Structure and Function of Biological Membranes. Belgium. | |
| dc.description | Fil: 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 | Fil: Inda, María Eugenia. Massachusetts Institute of Technology. Department of Electrical Engineering and Computer Science. Research Laboratory of Electronics. Cambridge. | |
| dc.description | Fil: Inda, María Eugenia. Massachusetts Institute of Technology. MIT Synthetic Biology Center. Cambridge. | |
| dc.description | Fil:Cybulski, Larisa Estefanía. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología. Argentina. | |
| dc.format | application/pdf | |
| dc.language | eng | |
| dc.publisher | MDPI | |
| dc.relation | https://www.mdpi.com/2218-273X/11/7/938 | |
| dc.relation | https://doi.org/10.3390/biom11070938 | |
| dc.rights | https://creativecommons.org/licenses/by/4.0/ | |
| dc.rights | Almada, Juan Cruz | |
| dc.rights | Bortolotti, Ana | |
| dc.rights | Ruysschaert, Jean Marie | |
| dc.rights | De Mendoza, Diego | |
| dc.rights | Inda, María Eugenia | |
| dc.rights | Cybulski, Larisa Estefanía | |
| dc.rights | Attribution 4.0 International (CC BY 4.0) | |
| dc.rights | openAccess | |
| dc.subject | Transmembrane Protein Interactions | |
| dc.subject | Hydrogen Bond Interaction | |
| dc.subject | Signal Transduction | |
| dc.subject | Histidine Kinase | |
| dc.subject | Dimerisation Motif | |
| dc.subject | Receptor | |
| dc.title | Interhelical h-bonds modulate the activity of a polytopic transmembrane kinase | |
| dc.type | publishedVersion | |
| dc.type | article | |
| dc.type | artículo | |
