Regulation of Bacillus subtilis DesK thermosensor by lipids

Temperature sensing is essential for the survival of living cells. The membrane-bound thermosensor DesK from Bacillus subtilis is a key representative of histidine kinases receptors able to remodel membrane lipid composition when the temperature drops below ∼30 ◦C. Although the receptor is well stud...

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Detalhes bibliográficos
Autores: Martín, Mariana, de Mendoza, Diego
Tipo de documento: artigo
Estado:Versão publicada
Data de publicação:2013
País:Argentina
Recursos:Consejo Nacional de Investigaciones Científicas y Técnicas
Repositório:CONICET Digital (CONICET)
Idioma:inglês
OAI Identifier:oai:ri.conicet.gov.ar:11336/3417
Acesso em linha:http://hdl.handle.net/11336/3417
Access Level:Acceso aberto
Palavra-chave:Desk
Thermosensor
Lipids
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
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spelling Regulation of Bacillus subtilis DesK thermosensor by lipidsMartín, Marianade Mendoza, DiegoDeskThermosensorLipidshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Temperature sensing is essential for the survival of living cells. The membrane-bound thermosensor DesK from Bacillus subtilis is a key representative of histidine kinases receptors able to remodel membrane lipid composition when the temperature drops below ∼30 ◦C. Although the receptor is well studied, a central issue remains: how does the compositional and functional diversity of the surrounding membrane modulate receptor function? Reconstituting full-length DesK into proteoliposomes of well-defined and controlled lipid composition represents a minimal synthetic approach to systematically address this question. Thus DesK has been reconstituted in a variety of phospholipid bilayers and its temperature-regulated autokinase activity determined as function of fatty acyl chain length, lipid head-group structure and phase preference. We show that the head group structure of lipids (both in vitro and in vivo) has little effect on DesK thermosensing, whereas properties determined by the acyl chain of lipids, such as membrane thickness and phase separation into coexisting lipid domains, exert a profound regulatory effect on kinase domain activation at low temperatures. These experiments suggest that the non-polar domain of glycerolipids is essential to regulate the allosteric structural transitions of DesK, by activating the autophosphorylation of the intracellular kinase domain in response to a decrease in temperature.Fil: Martín, Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; ArgentinaFil: de Mendoza, Diego. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); ArgentinaPortland Press2013-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/3417Martín, Mariana; de Mendoza, Diego; Regulation of Bacillus subtilis DesK thermosensor by lipids; Portland Press; Biochemical Journal; 1-2013; 269-2750264-6021enginfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2024-05-08T13:48:16Zoai:ri.conicet.gov.ar:11336/3417instacron: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:34982024-05-08 13:48:16.513CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Regulation of Bacillus subtilis DesK thermosensor by lipids
title Regulation of Bacillus subtilis DesK thermosensor by lipids
spellingShingle Regulation of Bacillus subtilis DesK thermosensor by lipids
Martín, Mariana
Desk
Thermosensor
Lipids
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
title_short Regulation of Bacillus subtilis DesK thermosensor by lipids
title_full Regulation of Bacillus subtilis DesK thermosensor by lipids
title_fullStr Regulation of Bacillus subtilis DesK thermosensor by lipids
title_full_unstemmed Regulation of Bacillus subtilis DesK thermosensor by lipids
title_sort Regulation of Bacillus subtilis DesK thermosensor by lipids
dc.creator.none.fl_str_mv Martín, Mariana
de Mendoza, Diego
author Martín, Mariana
author_facet Martín, Mariana
de Mendoza, Diego
author_role author
author2 de Mendoza, Diego
author2_role author
dc.subject.none.fl_str_mv Desk
Thermosensor
Lipids
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
topic Desk
Thermosensor
Lipids
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
description Temperature sensing is essential for the survival of living cells. The membrane-bound thermosensor DesK from Bacillus subtilis is a key representative of histidine kinases receptors able to remodel membrane lipid composition when the temperature drops below ∼30 ◦C. Although the receptor is well studied, a central issue remains: how does the compositional and functional diversity of the surrounding membrane modulate receptor function? Reconstituting full-length DesK into proteoliposomes of well-defined and controlled lipid composition represents a minimal synthetic approach to systematically address this question. Thus DesK has been reconstituted in a variety of phospholipid bilayers and its temperature-regulated autokinase activity determined as function of fatty acyl chain length, lipid head-group structure and phase preference. We show that the head group structure of lipids (both in vitro and in vivo) has little effect on DesK thermosensing, whereas properties determined by the acyl chain of lipids, such as membrane thickness and phase separation into coexisting lipid domains, exert a profound regulatory effect on kinase domain activation at low temperatures. These experiments suggest that the non-polar domain of glycerolipids is essential to regulate the allosteric structural transitions of DesK, by activating the autophosphorylation of the intracellular kinase domain in response to a decrease in temperature.
publishDate 2013
dc.date.none.fl_str_mv 2013-01
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/11336/3417
Martín, Mariana; de Mendoza, Diego; Regulation of Bacillus subtilis DesK thermosensor by lipids; Portland Press; Biochemical Journal; 1-2013; 269-275
0264-6021
url http://hdl.handle.net/11336/3417
identifier_str_mv Martín, Mariana; de Mendoza, Diego; Regulation of Bacillus subtilis DesK thermosensor by lipids; Portland Press; Biochemical Journal; 1-2013; 269-275
0264-6021
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Portland Press
publisher.none.fl_str_mv Portland Press
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
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_ 1799195292704178176
score 15,812429

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