Interhelical h-bonds modulate the activity of a polytopic transmembrane kinase
- Autores
- Almada, Juan Cruz; Bortolotti, Ana; Ruysschaert, Jean Marie; de Mendoza, Diego; Inda, María Eugenia; Cybulski, Larisa Estefania
- Año de publicación
- 2021
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- 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.
Fil: Almada, Juan Cruz. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina
Fil: Bortolotti, Ana. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina
Fil: Ruysschaert, Jean Marie. Université Libre de Bruxelles; Bélgica
Fil: de Mendoza, Diego. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Inda, María Eugenia. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología; Argentina. Massachusetts Institute of Technology; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina
Fil: Cybulski, Larisa Estefania. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina - Materia
-
DIMERISATION MOTIF
HISTIDINE KINASE
HYDROGEN BOND INTERACTION
RECEPTOR
SIGNAL TRANSDUCTION
TRANSMEMBRANE PROTEIN INTERACTIONS - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/153484
Ver los metadatos del registro completo
id |
CONICETDig_28fc3661a03f46343a512a35f017da95 |
---|---|
oai_identifier_str |
oai:ri.conicet.gov.ar:11336/153484 |
network_acronym_str |
CONICETDig |
repository_id_str |
3498 |
network_name_str |
CONICET Digital (CONICET) |
spelling |
Interhelical h-bonds modulate the activity of a polytopic transmembrane kinaseAlmada, Juan CruzBortolotti, AnaRuysschaert, Jean Mariede Mendoza, DiegoInda, María EugeniaCybulski, Larisa EstefaniaDIMERISATION MOTIFHISTIDINE KINASEHYDROGEN BOND INTERACTIONRECEPTORSIGNAL TRANSDUCTIONTRANSMEMBRANE PROTEIN INTERACTIONShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1DesK 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.Fil: Almada, Juan Cruz. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; ArgentinaFil: Bortolotti, Ana. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; ArgentinaFil: Ruysschaert, Jean Marie. Université Libre de Bruxelles; BélgicaFil: de Mendoza, Diego. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Inda, María Eugenia. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología; Argentina. Massachusetts Institute of Technology; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; ArgentinaFil: Cybulski, Larisa Estefania. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; ArgentinaMultidisciplinary Digital Publishing Institute2021-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/153484Almada, 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; 1-122218-273X2218-273XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/info:eu-repo/semantics/altIdentifier/doi/10.3390/biom11070938info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:07:03Zoai:ri.conicet.gov.ar:11336/153484instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 10:07:03.423CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Interhelical h-bonds modulate the activity of a polytopic transmembrane kinase |
title |
Interhelical h-bonds modulate the activity of a polytopic transmembrane kinase |
spellingShingle |
Interhelical h-bonds modulate the activity of a polytopic transmembrane kinase Almada, Juan Cruz DIMERISATION MOTIF HISTIDINE KINASE HYDROGEN BOND INTERACTION RECEPTOR SIGNAL TRANSDUCTION TRANSMEMBRANE PROTEIN INTERACTIONS |
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 |
dc.creator.none.fl_str_mv |
Almada, Juan Cruz Bortolotti, Ana Ruysschaert, Jean Marie de Mendoza, Diego Inda, María Eugenia Cybulski, Larisa Estefania |
author |
Almada, Juan Cruz |
author_facet |
Almada, Juan Cruz Bortolotti, Ana Ruysschaert, Jean Marie de Mendoza, Diego Inda, María Eugenia Cybulski, Larisa Estefania |
author_role |
author |
author2 |
Bortolotti, Ana Ruysschaert, Jean Marie de Mendoza, Diego Inda, María Eugenia Cybulski, Larisa Estefania |
author2_role |
author author author author author |
dc.subject.none.fl_str_mv |
DIMERISATION MOTIF HISTIDINE KINASE HYDROGEN BOND INTERACTION RECEPTOR SIGNAL TRANSDUCTION TRANSMEMBRANE PROTEIN INTERACTIONS |
topic |
DIMERISATION MOTIF HISTIDINE KINASE HYDROGEN BOND INTERACTION RECEPTOR SIGNAL TRANSDUCTION TRANSMEMBRANE PROTEIN INTERACTIONS |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
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. Fil: Almada, Juan Cruz. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina Fil: Bortolotti, Ana. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina Fil: Ruysschaert, Jean Marie. Université Libre de Bruxelles; Bélgica Fil: de Mendoza, Diego. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina Fil: Inda, María Eugenia. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología; Argentina. Massachusetts Institute of Technology; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina Fil: Cybulski, Larisa Estefania. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina |
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. |
publishDate |
2021 |
dc.date.none.fl_str_mv |
2021-07 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
format |
article |
status_str |
publishedVersion |
dc.identifier.none.fl_str_mv |
http://hdl.handle.net/11336/153484 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 |
url |
http://hdl.handle.net/11336/153484 |
identifier_str_mv |
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 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/doi/ info:eu-repo/semantics/altIdentifier/doi/10.3390/biom11070938 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Multidisciplinary Digital Publishing Institute |
publisher.none.fl_str_mv |
Multidisciplinary Digital Publishing Institute |
dc.source.none.fl_str_mv |
reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
reponame_str |
CONICET Digital (CONICET) |
collection |
CONICET Digital (CONICET) |
instname_str |
Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.name.fl_str_mv |
CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.mail.fl_str_mv |
dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
_version_ |
1844613925660786688 |
score |
13.070432 |