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...
Guardado en:
| Autores principales: | , , , , |
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| Formato: | article artículo publishedVersion |
| Lenguaje: | Inglés |
| Publicado: |
MDPI
2022
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| Materias: | |
| Acceso en línea: | http://hdl.handle.net/2133/23273 http://hdl.handle.net/2133/23273 |
| Aporte de: |
| 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 |
| work_keys_str_mv |
AT almadajuancruz interhelicalhbondsmodulatetheactivityofapolytopictransmembranekinase AT bortolottiana interhelicalhbondsmodulatetheactivityofapolytopictransmembranekinase AT ruysschaertjanemarie interhelicalhbondsmodulatetheactivityofapolytopictransmembranekinase AT demendozadiego interhelicalhbondsmodulatetheactivityofapolytopictransmembranekinase AT cybulskilarisaestefania interhelicalhbondsmodulatetheactivityofapolytopictransmembranekinase |
| bdutipo_str |
Repositorios |
| _version_ |
1764820411907833860 |