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
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/153484
Acceder
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 Técnicas2025-10-22T11:36:57Zoai: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:34982025-10-22 11:36:58.023CONICET 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_ 1846782014780342272
score 12.982451

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