Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 1 de 1
Filtrar
Más filtros











Base de datos
Intervalo de año de publicación
1.
Mol Microbiol ; 98(2): 258-71, 2015 Oct.
Artículo en Inglés | MEDLINE | ID: mdl-26172072

RESUMEN

The thermosensor histidine kinase DesK from Bacillus subtilis senses changes in membrane fluidity initiating an adaptive response. Structural changes in DesK have been implicated in transmembrane signaling, but direct evidence is still lacking. On the basis of structure-guided mutagenesis, we now propose a mechanism of DesK-mediated signal sensing and transduction. The data indicate that stabilization/destabilization of a 2-helix coiled coil, which connects the transmembrane sensory domain of DesK to its cytosolic catalytic region, is crucial to control its signaling state. Computational modeling and simulations reveal couplings between protein, water and membrane mechanics. We propose that membrane thickening is the main driving force for signal sensing and that it acts by inducing helix stretching and rotation prompting an asymmetric kinase-competent state. Overall, the known structural changes of the sensor kinase, as well as further dynamic rearrangements that we now predict, consistently link structure determinants to activity modulation.


Asunto(s)
Bacillus subtilis/fisiología , Proteínas Bacterianas/química , Proteínas Bacterianas/metabolismo , Proteínas Quinasas/química , Proteínas Quinasas/metabolismo , Transducción de Señal , Bacillus subtilis/enzimología , Bacillus subtilis/genética , Membrana Celular/metabolismo , Frío , Simulación por Computador , Histidina Quinasa , Fluidez de la Membrana , Proteínas de la Membrana/metabolismo , Mutagénesis , Conformación Proteica , Proteínas Quinasas/genética , Transducción de Señal/genética
SELECCIÓN DE REFERENCIAS
DETALLE DE LA BÚSQUEDA