info:eu-repo/semantics/article
Interhelical h-bonds modulate the activity of a polytopic transmembrane kinase
Fecha
2021-07Registro en:
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
2218-273X
2218-273X
CONICET Digital
CONICET
Autor
Almada, Juan Cruz
Bortolotti, Ana
Ruysschaert, Jean Marie
de Mendoza, Diego
Inda, María Eugenia
Cybulski, Larisa Estefania
Resumen
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.