2022-03-282022-03-2820212218-273Xhttp://hdl.handle.net/2133/23273DesK 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.application/pdf1-12engopenAccessTransmembrane Protein InteractionsHydrogen Bond InteractionSignal TransductionHistidine KinaseDimerisation MotifReceptorpublishedVersionAlmada, Juan CruzBortolotti, AnaRuysschaert, Jean MarieDe Mendoza, DiegoInda, María EugeniaCybulski, Larisa EstefaníaAttribution 4.0 International (CC BY 4.0)