ExoS/ChvI two-component signal-transduction system activated in the absence of bacterial phosphatidylcholine

Autores
Geiger, Otto; Sohlenkamp, Christian; Vera-Cruz, Diana; Medeot, Daniela Beatriz; Martínez-Aguilar, Lourdes; Sahonero-Canavesi, Diana X.; Weidner, Stefan; Pühler, Alfred; López Lara, Isabel M.
Año de publicación
2021
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Sinorhizobium meliloti contains the negatively charged phosphatidylglycerol and cardiolipin as well as the zwitterionic phosphatidylethanolamine (PE) and phosphatidylcholine (PC) as major membrane phospholipids. In previous studies we had isolated S. meliloti mutants that lack PE or PC. Although mutants deficient in PE are able to form nitrogen-fixing nodules on alfalfa host plants, mutants lacking PC cannot sustain development of any nodules on host roots. Transcript profiles of mutants unable to form PE or PC are distinct; they differ from each other and they are different from the wild type profile. For example, a PC-deficient mutant of S. meliloti shows an increase of transcripts that encode enzymes required for succinoglycan biosynthesis and a decrease of transcripts required for flagellum formation. Indeed, a PC-deficient mutant is unable to swim and overproduces succinoglycan. Some suppressor mutants, that regain swimming and form normal levels of succinoglycan, are altered in the ExoS sensor. Our findings suggest that the lack of PC in the sinorhizobial membrane activates the ExoS/ChvI two-component regulatory system. ExoS/ChvI constitute a molecular switch in S. meliloti for changing from a free-living to a symbiotic life style. The periplasmic repressor protein ExoR controls ExoS/ChvI function and it is thought that proteolytic ExoR degradation would relieve repression of ExoS/ChvI thereby switching on this system. However, as ExoR levels are similar in wild type, PC-deficient mutant and suppressor mutants, we propose that lack of PC in the bacterial membrane provokes directly a conformational change of the ExoS sensor and thereby activation of the ExoS/ChvI two-component system.
Fil: Geiger, Otto. Universidad Nacional Autónoma de México; México
Fil: Sohlenkamp, Christian. Universidad Nacional Autónoma de México; México
Fil: Vera-Cruz, Diana. Universidad Nacional Autónoma de México; México
Fil: Medeot, Daniela Beatriz. Universidad Nacional Autónoma de México; México. Universidad Nacional de Rio Cuarto. Facultad de Cs.exactas Fisicoquimicas y Naturales. Instituto de Biotecnologia Ambiental y Salud. - Consejo Nacional de Investigaciones Cientificas y Tecnicas. Centro Cientifico Tecnologico Conicet - Cordoba. Instituto de Biotecnologia Ambiental y Salud.; Argentina
Fil: Martínez-Aguilar, Lourdes. Universidad Nacional Autónoma de México; México
Fil: Sahonero-Canavesi, Diana X.. Universidad Nacional Autónoma de México; México
Fil: Weidner, Stefan. Universitaet Biehlefeld; Alemania
Fil: Pühler, Alfred. Universitaet Biehlefeld; Alemania
Fil: López Lara, Isabel M.. Universidad Nacional Autónoma de México; México
Materia
MEMBRANE LIPID
MOTILITY
PHOSPHATIDYLETHANOLAMINE
SINORHIZOBIUM MELILOTI
SUCCINOGLYCAN
SYMBIOSIS
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/181484
Acceder
id CONICETDig_5a97a774c39a39b90e0ad81054f14906
oai_identifier_str oai:ri.conicet.gov.ar:11336/181484
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling ExoS/ChvI two-component signal-transduction system activated in the absence of bacterial phosphatidylcholineGeiger, OttoSohlenkamp, ChristianVera-Cruz, DianaMedeot, Daniela BeatrizMartínez-Aguilar, LourdesSahonero-Canavesi, Diana X.Weidner, StefanPühler, AlfredLópez Lara, Isabel M.MEMBRANE LIPIDMOTILITYPHOSPHATIDYLETHANOLAMINESINORHIZOBIUM MELILOTISUCCINOGLYCANSYMBIOSIShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Sinorhizobium meliloti contains the negatively charged phosphatidylglycerol and cardiolipin as well as the zwitterionic phosphatidylethanolamine (PE) and phosphatidylcholine (PC) as major membrane phospholipids. In previous studies we had isolated S. meliloti mutants that lack PE or PC. Although mutants deficient in PE are able to form nitrogen-fixing nodules on alfalfa host plants, mutants lacking PC cannot sustain development of any nodules on host roots. Transcript profiles of mutants unable to form PE or PC are distinct; they differ from each other and they are different from the wild type profile. For example, a PC-deficient mutant of S. meliloti shows an increase of transcripts that encode enzymes required for succinoglycan biosynthesis and a decrease of transcripts required for flagellum formation. Indeed, a PC-deficient mutant is unable to swim and overproduces succinoglycan. Some suppressor mutants, that regain swimming and form normal levels of succinoglycan, are altered in the ExoS sensor. Our findings suggest that the lack of PC in the sinorhizobial membrane activates the ExoS/ChvI two-component regulatory system. ExoS/ChvI constitute a molecular switch in S. meliloti for changing from a free-living to a symbiotic life style. The periplasmic repressor protein ExoR controls ExoS/ChvI function and it is thought that proteolytic ExoR degradation would relieve repression of ExoS/ChvI thereby switching on this system. However, as ExoR levels are similar in wild type, PC-deficient mutant and suppressor mutants, we propose that lack of PC in the bacterial membrane provokes directly a conformational change of the ExoS sensor and thereby activation of the ExoS/ChvI two-component system.Fil: Geiger, Otto. Universidad Nacional Autónoma de México; MéxicoFil: Sohlenkamp, Christian. Universidad Nacional Autónoma de México; MéxicoFil: Vera-Cruz, Diana. Universidad Nacional Autónoma de México; MéxicoFil: Medeot, Daniela Beatriz. Universidad Nacional Autónoma de México; México. Universidad Nacional de Rio Cuarto. Facultad de Cs.exactas Fisicoquimicas y Naturales. Instituto de Biotecnologia Ambiental y Salud. - Consejo Nacional de Investigaciones Cientificas y Tecnicas. Centro Cientifico Tecnologico Conicet - Cordoba. Instituto de Biotecnologia Ambiental y Salud.; ArgentinaFil: Martínez-Aguilar, Lourdes. Universidad Nacional Autónoma de México; MéxicoFil: Sahonero-Canavesi, Diana X.. Universidad Nacional Autónoma de México; MéxicoFil: Weidner, Stefan. Universitaet Biehlefeld; AlemaniaFil: Pühler, Alfred. Universitaet Biehlefeld; AlemaniaFil: López Lara, Isabel M.. Universidad Nacional Autónoma de México; MéxicoFrontiers Media S.A.2021-07-23info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/181484Geiger, Otto; Sohlenkamp, Christian; Vera-Cruz, Diana; Medeot, Daniela Beatriz; Martínez-Aguilar, Lourdes; et al.; ExoS/ChvI two-component signal-transduction system activated in the absence of bacterial phosphatidylcholine; Frontiers Media S.A.; Frontiers in Plant Science; 12; 23-7-2021; 1-201664-462XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.frontiersin.org/articles/10.3389/fpls.2021.678976/fullinfo:eu-repo/semantics/altIdentifier/doi/10.3389/fpls.2021.678976info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:07:08Zoai:ri.conicet.gov.ar:11336/181484instacron: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 10:07:09.021CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv ExoS/ChvI two-component signal-transduction system activated in the absence of bacterial phosphatidylcholine
title ExoS/ChvI two-component signal-transduction system activated in the absence of bacterial phosphatidylcholine
spellingShingle ExoS/ChvI two-component signal-transduction system activated in the absence of bacterial phosphatidylcholine
Geiger, Otto
MEMBRANE LIPID
MOTILITY
PHOSPHATIDYLETHANOLAMINE
SINORHIZOBIUM MELILOTI
SUCCINOGLYCAN
SYMBIOSIS
title_short ExoS/ChvI two-component signal-transduction system activated in the absence of bacterial phosphatidylcholine
title_full ExoS/ChvI two-component signal-transduction system activated in the absence of bacterial phosphatidylcholine
title_fullStr ExoS/ChvI two-component signal-transduction system activated in the absence of bacterial phosphatidylcholine
title_full_unstemmed ExoS/ChvI two-component signal-transduction system activated in the absence of bacterial phosphatidylcholine
title_sort ExoS/ChvI two-component signal-transduction system activated in the absence of bacterial phosphatidylcholine
dc.creator.none.fl_str_mv Geiger, Otto
Sohlenkamp, Christian
Vera-Cruz, Diana
Medeot, Daniela Beatriz
Martínez-Aguilar, Lourdes
Sahonero-Canavesi, Diana X.
Weidner, Stefan
Pühler, Alfred
López Lara, Isabel M.
author Geiger, Otto
author_facet Geiger, Otto
Sohlenkamp, Christian
Vera-Cruz, Diana
Medeot, Daniela Beatriz
Martínez-Aguilar, Lourdes
Sahonero-Canavesi, Diana X.
Weidner, Stefan
Pühler, Alfred
López Lara, Isabel M.
author_role author
author2 Sohlenkamp, Christian
Vera-Cruz, Diana
Medeot, Daniela Beatriz
Martínez-Aguilar, Lourdes
Sahonero-Canavesi, Diana X.
Weidner, Stefan
Pühler, Alfred
López Lara, Isabel M.
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv MEMBRANE LIPID
MOTILITY
PHOSPHATIDYLETHANOLAMINE
SINORHIZOBIUM MELILOTI
SUCCINOGLYCAN
SYMBIOSIS
topic MEMBRANE LIPID
MOTILITY
PHOSPHATIDYLETHANOLAMINE
SINORHIZOBIUM MELILOTI
SUCCINOGLYCAN
SYMBIOSIS
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Sinorhizobium meliloti contains the negatively charged phosphatidylglycerol and cardiolipin as well as the zwitterionic phosphatidylethanolamine (PE) and phosphatidylcholine (PC) as major membrane phospholipids. In previous studies we had isolated S. meliloti mutants that lack PE or PC. Although mutants deficient in PE are able to form nitrogen-fixing nodules on alfalfa host plants, mutants lacking PC cannot sustain development of any nodules on host roots. Transcript profiles of mutants unable to form PE or PC are distinct; they differ from each other and they are different from the wild type profile. For example, a PC-deficient mutant of S. meliloti shows an increase of transcripts that encode enzymes required for succinoglycan biosynthesis and a decrease of transcripts required for flagellum formation. Indeed, a PC-deficient mutant is unable to swim and overproduces succinoglycan. Some suppressor mutants, that regain swimming and form normal levels of succinoglycan, are altered in the ExoS sensor. Our findings suggest that the lack of PC in the sinorhizobial membrane activates the ExoS/ChvI two-component regulatory system. ExoS/ChvI constitute a molecular switch in S. meliloti for changing from a free-living to a symbiotic life style. The periplasmic repressor protein ExoR controls ExoS/ChvI function and it is thought that proteolytic ExoR degradation would relieve repression of ExoS/ChvI thereby switching on this system. However, as ExoR levels are similar in wild type, PC-deficient mutant and suppressor mutants, we propose that lack of PC in the bacterial membrane provokes directly a conformational change of the ExoS sensor and thereby activation of the ExoS/ChvI two-component system.
Fil: Geiger, Otto. Universidad Nacional Autónoma de México; México
Fil: Sohlenkamp, Christian. Universidad Nacional Autónoma de México; México
Fil: Vera-Cruz, Diana. Universidad Nacional Autónoma de México; México
Fil: Medeot, Daniela Beatriz. Universidad Nacional Autónoma de México; México. Universidad Nacional de Rio Cuarto. Facultad de Cs.exactas Fisicoquimicas y Naturales. Instituto de Biotecnologia Ambiental y Salud. - Consejo Nacional de Investigaciones Cientificas y Tecnicas. Centro Cientifico Tecnologico Conicet - Cordoba. Instituto de Biotecnologia Ambiental y Salud.; Argentina
Fil: Martínez-Aguilar, Lourdes. Universidad Nacional Autónoma de México; México
Fil: Sahonero-Canavesi, Diana X.. Universidad Nacional Autónoma de México; México
Fil: Weidner, Stefan. Universitaet Biehlefeld; Alemania
Fil: Pühler, Alfred. Universitaet Biehlefeld; Alemania
Fil: López Lara, Isabel M.. Universidad Nacional Autónoma de México; México
description Sinorhizobium meliloti contains the negatively charged phosphatidylglycerol and cardiolipin as well as the zwitterionic phosphatidylethanolamine (PE) and phosphatidylcholine (PC) as major membrane phospholipids. In previous studies we had isolated S. meliloti mutants that lack PE or PC. Although mutants deficient in PE are able to form nitrogen-fixing nodules on alfalfa host plants, mutants lacking PC cannot sustain development of any nodules on host roots. Transcript profiles of mutants unable to form PE or PC are distinct; they differ from each other and they are different from the wild type profile. For example, a PC-deficient mutant of S. meliloti shows an increase of transcripts that encode enzymes required for succinoglycan biosynthesis and a decrease of transcripts required for flagellum formation. Indeed, a PC-deficient mutant is unable to swim and overproduces succinoglycan. Some suppressor mutants, that regain swimming and form normal levels of succinoglycan, are altered in the ExoS sensor. Our findings suggest that the lack of PC in the sinorhizobial membrane activates the ExoS/ChvI two-component regulatory system. ExoS/ChvI constitute a molecular switch in S. meliloti for changing from a free-living to a symbiotic life style. The periplasmic repressor protein ExoR controls ExoS/ChvI function and it is thought that proteolytic ExoR degradation would relieve repression of ExoS/ChvI thereby switching on this system. However, as ExoR levels are similar in wild type, PC-deficient mutant and suppressor mutants, we propose that lack of PC in the bacterial membrane provokes directly a conformational change of the ExoS sensor and thereby activation of the ExoS/ChvI two-component system.
publishDate 2021
dc.date.none.fl_str_mv 2021-07-23
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/11336/181484
Geiger, Otto; Sohlenkamp, Christian; Vera-Cruz, Diana; Medeot, Daniela Beatriz; Martínez-Aguilar, Lourdes; et al.; ExoS/ChvI two-component signal-transduction system activated in the absence of bacterial phosphatidylcholine; Frontiers Media S.A.; Frontiers in Plant Science; 12; 23-7-2021; 1-20
1664-462X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/181484
identifier_str_mv Geiger, Otto; Sohlenkamp, Christian; Vera-Cruz, Diana; Medeot, Daniela Beatriz; Martínez-Aguilar, Lourdes; et al.; ExoS/ChvI two-component signal-transduction system activated in the absence of bacterial phosphatidylcholine; Frontiers Media S.A.; Frontiers in Plant Science; 12; 23-7-2021; 1-20
1664-462X
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.frontiersin.org/articles/10.3389/fpls.2021.678976/full
info:eu-repo/semantics/altIdentifier/doi/10.3389/fpls.2021.678976
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Frontiers Media S.A.
publisher.none.fl_str_mv Frontiers Media S.A.
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
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score 13.070432

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