A transmembrane Histidine Kinase functions as a pH sensor

The two-component system DesK-DesR regulates the synthesis of unsaturated fatty acids in the soil bacteria Bacillus subtilis. This system is activated at low temperature and maintains membrane lipid fluidity upon temperature variations. Here, we found that DesK—the transmembrane histidine kinase—...

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Autores principales: Bortolotti, Ana, Vazquez, Daniela Belén, Almada, Juan Cruz, Inda, María Eugenia, Drusin, Salvador Iván, Villalba, Juan Manuel, Moreno, Diego M., Ruysschaert, Jean Marie, Cybulski, Larisa Estefanía
Formato: article artículo publishedVersion
Lenguaje:Inglés
Publicado: MDPI 2021
Materias:
Helix Stabilization
PH Sensor
Coulomb Interactions
Acceso en línea:http://hdl.handle.net/2133/20490
http://hdl.handle.net/2133/20490
Aporte de:
Repositorio Hipermedial de la Universidad Nacional de Rosario (UNR) de Universidad Nacional de Rosario
id I15-R121-2133-20490
record_format dspace
institution Universidad Nacional de Rosario
institution_str I-15
repository_str R-121
collection Repositorio Hipermedial de la Universidad Nacional de Rosario (UNR)
language Inglés
orig_language_str_mv eng
topic Helix Stabilization
PH Sensor
Coulomb Interactions
spellingShingle Helix Stabilization
PH Sensor
Coulomb Interactions
Bortolotti, Ana
Vazquez, Daniela Belén
Almada, Juan Cruz
Inda, María Eugenia
Drusin, Salvador Iván
Villalba, Juan Manuel
Moreno, Diego M.
Ruysschaert, Jean Marie
Cybulski, Larisa Estefanía
A transmembrane Histidine Kinase functions as a pH sensor
topic_facet Helix Stabilization
PH Sensor
Coulomb Interactions
description The two-component system DesK-DesR regulates the synthesis of unsaturated fatty acids in the soil bacteria Bacillus subtilis. This system is activated at low temperature and maintains membrane lipid fluidity upon temperature variations. Here, we found that DesK—the transmembrane histidine kinase—also responds to pH and studied the mechanism of pH sensing. We propose that a helix linking the transmembrane region with the cytoplasmic catalytic domain is involved in pH sensing. This helix contains several glutamate, lysine, and arginine residues At neutral pH, the linker forms an alpha helix that is stabilized by hydrogen bonds in the i, i + 4 register and thus favors the kinase state. At low pH, protonation of glutamate residues breaks salt bridges, which results in helix destabilization and interruption of signaling. This mechanism inhibits unsaturated fatty acid synthesis and rigidifies the membrane when Bacillus grows in acidic conditions.
format article
artículo
publishedVersion
author Bortolotti, Ana
Vazquez, Daniela Belén
Almada, Juan Cruz
Inda, María Eugenia
Drusin, Salvador Iván
Villalba, Juan Manuel
Moreno, Diego M.
Ruysschaert, Jean Marie
Cybulski, Larisa Estefanía
author_facet Bortolotti, Ana
Vazquez, Daniela Belén
Almada, Juan Cruz
Inda, María Eugenia
Drusin, Salvador Iván
Villalba, Juan Manuel
Moreno, Diego M.
Ruysschaert, Jean Marie
Cybulski, Larisa Estefanía
author_sort Bortolotti, Ana
title A transmembrane Histidine Kinase functions as a pH sensor
title_short A transmembrane Histidine Kinase functions as a pH sensor
title_full A transmembrane Histidine Kinase functions as a pH sensor
title_fullStr A transmembrane Histidine Kinase functions as a pH sensor
title_full_unstemmed A transmembrane Histidine Kinase functions as a pH sensor
title_sort transmembrane histidine kinase functions as a ph sensor
publisher MDPI
publishDate 2021
url http://hdl.handle.net/2133/20490
http://hdl.handle.net/2133/20490
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