Interhelical H-Bonds Modulate the Activity of a Polytopic Transmembrane Kinase

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 catalyt...

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Detalles Bibliográficos
Autores principales: Almada, Juan Cruz, Bortolotti, Ana, Ruysschaert, Jane Marie, De Mendoza, Diego, Cybulski, Larisa Estefanía
Formato: article artículo publishedVersion
Lenguaje:Inglés
Publicado: MDPI 2022
Materias:
Transmembrane Protein Interactions
Hydrogen Bond Interaction
Signal Transduction
Histidine Kinase
Dimerisation Motif
Receptor
Acceso en línea:http://hdl.handle.net/2133/23273
http://hdl.handle.net/2133/23273
Aporte de:
Repositorio Hipermedial de la Universidad Nacional de Rosario (UNR) de Universidad Nacional de Rosario
id I15-R121-2133-23273
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 Transmembrane Protein Interactions
Hydrogen Bond Interaction
Signal Transduction
Histidine Kinase
Dimerisation Motif
Receptor
spellingShingle Transmembrane Protein Interactions
Hydrogen Bond Interaction
Signal Transduction
Histidine Kinase
Dimerisation Motif
Receptor
Almada, Juan Cruz
Bortolotti, Ana
Ruysschaert, Jane Marie
De Mendoza, Diego
Cybulski, Larisa Estefanía
Interhelical H-Bonds Modulate the Activity of a Polytopic Transmembrane Kinase
topic_facet Transmembrane Protein Interactions
Hydrogen Bond Interaction
Signal Transduction
Histidine Kinase
Dimerisation Motif
Receptor
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.
format article
artículo
publishedVersion
author Almada, Juan Cruz
Bortolotti, Ana
Ruysschaert, Jane Marie
De Mendoza, Diego
Cybulski, Larisa Estefanía
author_facet Almada, Juan Cruz
Bortolotti, Ana
Ruysschaert, Jane Marie
De Mendoza, Diego
Cybulski, Larisa Estefanía
author_sort Almada, Juan Cruz
title Interhelical H-Bonds Modulate the Activity of a Polytopic Transmembrane Kinase
title_short Interhelical H-Bonds Modulate the Activity of a Polytopic Transmembrane Kinase
title_full Interhelical H-Bonds Modulate the Activity of a Polytopic Transmembrane Kinase
title_fullStr Interhelical H-Bonds Modulate the Activity of a Polytopic Transmembrane Kinase
title_full_unstemmed Interhelical H-Bonds Modulate the Activity of a Polytopic Transmembrane Kinase
title_sort interhelical h-bonds modulate the activity of a polytopic transmembrane kinase
publisher MDPI
publishDate 2022
url http://hdl.handle.net/2133/23273
http://hdl.handle.net/2133/23273
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AT bortolottiana interhelicalhbondsmodulatetheactivityofapolytopictransmembranekinase
AT ruysschaertjanemarie interhelicalhbondsmodulatetheactivityofapolytopictransmembranekinase
AT demendozadiego interhelicalhbondsmodulatetheactivityofapolytopictransmembranekinase
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bdutipo_str Repositorios
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