Light regulates attachment, exopolysaccharide production, and nodulation in Rhizobium leguminosarum through a LOV-histidine kinase photoreceptor

Autores
Bonomi, H.R.; Posadas, D.M.; Paris, G.; Del Carmen Carrica, M.; Frederickson, M.; Pietrasanta, L.I.; Bogomolni, R.A.; Zorreguieta, A.; Goldbaum, F.A.
Año de publicación
2012
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Rhizobium leguminosarum is a soil bacterium that infects root hairs and induces the formation of nitrogen-fixing nodules on leguminous plants. Light, oxygen, and voltage (LOV)-domain proteins are bluelight receptors found in higher plants and many algae, fungi, and bacteria. The genome of R. leguminosarum bv. viciae 3841, a peanodulating endosymbiont, encodes a sensor histidine kinase containing a LOV domain at the N-terminal end (R-LOV-HK). R-LOV-HK has a typical LOV domain absorption spectrum with broad bands in the blue and UV-A regions and shows a truncated photocycle. Here we show that the R-LOV-HK protein regulates attachment to an abiotic surface and production of flagellar proteins and exopolysaccharide in response to light. Also, illumination of bacterial cultures before inoculation of pea roots increases the number of nodules per plant and the number of intranodular bacteroids. The effects of light on nodulation are dependent on a functional lov gene. The results presented in this work suggest that light, sensed by R-LOV-HK, is an important environmental factor that controls adaptive responses and the symbiotic efficiency of R. leguminosarum.
Fil:Posadas, D.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Zorreguieta, A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fuente
Proc. Natl. Acad. Sci. U. S. A. 2012;109(30):12135-12140
Materia
bacterial polysaccharide
bacterial protein
exopolysaccharide
light oxygen and voltage histidine kinase
unclassified drug
adaptation
amino terminal sequence
article
bacterial gene
bacterium culture
biofilm
blue light
environmental factor
illumination
light
lov gene
nodulation
nonhuman
pea
plant root
priority journal
protein synthesis
real time polymerase chain reaction
reverse transcription polymerase chain reaction
Rhizobium leguminosarum
symbiosis
Amino Acid Sequence
Bacterial Adhesion
Base Sequence
Biofilms
Blotting, Western
Flagella
Gentian Violet
Light
Microscopy, Electron, Scanning
Molecular Sequence Data
Peas
Photoreceptors, Microbial
Plant Root Nodulation
Polysaccharides, Bacterial
Protein Kinases
Protein Structure, Tertiary
Real-Time Polymerase Chain Reaction
Rhizobium leguminosarum
Sequence Alignment
Sequence Analysis, DNA
Statistics, Nonparametric
Symbiosis
algae
Bacteria (microorganisms)
Embryophyta
Fabaceae
Fungi
Pisum sativum
Rhizobium leguminosarum
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/2.5/ar
Repositorio
Biblioteca Digital (UBA-FCEN)
Institución
Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
OAI Identificador
paperaa:paper_00278424_v109_n30_p12135_Bonomi

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oai_identifier_str paperaa:paper_00278424_v109_n30_p12135_Bonomi
network_acronym_str BDUBAFCEN
repository_id_str 1896
network_name_str Biblioteca Digital (UBA-FCEN)
spelling Light regulates attachment, exopolysaccharide production, and nodulation in Rhizobium leguminosarum through a LOV-histidine kinase photoreceptorBonomi, H.R.Posadas, D.M.Paris, G.Del Carmen Carrica, M.Frederickson, M.Pietrasanta, L.I.Bogomolni, R.A.Zorreguieta, A.Goldbaum, F.A.bacterial polysaccharidebacterial proteinexopolysaccharidelight oxygen and voltage histidine kinaseunclassified drugadaptationamino terminal sequencearticlebacterial genebacterium culturebiofilmblue lightenvironmental factorilluminationlightlov genenodulationnonhumanpeaplant rootpriority journalprotein synthesisreal time polymerase chain reactionreverse transcription polymerase chain reactionRhizobium leguminosarumsymbiosisAmino Acid SequenceBacterial AdhesionBase SequenceBiofilmsBlotting, WesternFlagellaGentian VioletLightMicroscopy, Electron, ScanningMolecular Sequence DataPeasPhotoreceptors, MicrobialPlant Root NodulationPolysaccharides, BacterialProtein KinasesProtein Structure, TertiaryReal-Time Polymerase Chain ReactionRhizobium leguminosarumSequence AlignmentSequence Analysis, DNAStatistics, NonparametricSymbiosisalgaeBacteria (microorganisms)EmbryophytaFabaceaeFungiPisum sativumRhizobium leguminosarumRhizobium leguminosarum is a soil bacterium that infects root hairs and induces the formation of nitrogen-fixing nodules on leguminous plants. Light, oxygen, and voltage (LOV)-domain proteins are bluelight receptors found in higher plants and many algae, fungi, and bacteria. The genome of R. leguminosarum bv. viciae 3841, a peanodulating endosymbiont, encodes a sensor histidine kinase containing a LOV domain at the N-terminal end (R-LOV-HK). R-LOV-HK has a typical LOV domain absorption spectrum with broad bands in the blue and UV-A regions and shows a truncated photocycle. Here we show that the R-LOV-HK protein regulates attachment to an abiotic surface and production of flagellar proteins and exopolysaccharide in response to light. Also, illumination of bacterial cultures before inoculation of pea roots increases the number of nodules per plant and the number of intranodular bacteroids. The effects of light on nodulation are dependent on a functional lov gene. The results presented in this work suggest that light, sensed by R-LOV-HK, is an important environmental factor that controls adaptive responses and the symbiotic efficiency of R. leguminosarum.Fil:Posadas, D.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Zorreguieta, A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.2012info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://hdl.handle.net/20.500.12110/paper_00278424_v109_n30_p12135_BonomiProc. Natl. Acad. Sci. U. S. A. 2012;109(30):12135-12140reponame:Biblioteca Digital (UBA-FCEN)instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesinstacron:UBA-FCENenginfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/2.5/ar2025-09-11T10:21:47Zpaperaa:paper_00278424_v109_n30_p12135_BonomiInstitucionalhttps://digital.bl.fcen.uba.ar/Universidad públicaNo correspondehttps://digital.bl.fcen.uba.ar/cgi-bin/oaiserver.cgiana@bl.fcen.uba.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:18962025-09-11 10:21:49.394Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesfalse
dc.title.none.fl_str_mv Light regulates attachment, exopolysaccharide production, and nodulation in Rhizobium leguminosarum through a LOV-histidine kinase photoreceptor
title Light regulates attachment, exopolysaccharide production, and nodulation in Rhizobium leguminosarum through a LOV-histidine kinase photoreceptor
spellingShingle Light regulates attachment, exopolysaccharide production, and nodulation in Rhizobium leguminosarum through a LOV-histidine kinase photoreceptor
Bonomi, H.R.
bacterial polysaccharide
bacterial protein
exopolysaccharide
light oxygen and voltage histidine kinase
unclassified drug
adaptation
amino terminal sequence
article
bacterial gene
bacterium culture
biofilm
blue light
environmental factor
illumination
light
lov gene
nodulation
nonhuman
pea
plant root
priority journal
protein synthesis
real time polymerase chain reaction
reverse transcription polymerase chain reaction
Rhizobium leguminosarum
symbiosis
Amino Acid Sequence
Bacterial Adhesion
Base Sequence
Biofilms
Blotting, Western
Flagella
Gentian Violet
Light
Microscopy, Electron, Scanning
Molecular Sequence Data
Peas
Photoreceptors, Microbial
Plant Root Nodulation
Polysaccharides, Bacterial
Protein Kinases
Protein Structure, Tertiary
Real-Time Polymerase Chain Reaction
Rhizobium leguminosarum
Sequence Alignment
Sequence Analysis, DNA
Statistics, Nonparametric
Symbiosis
algae
Bacteria (microorganisms)
Embryophyta
Fabaceae
Fungi
Pisum sativum
Rhizobium leguminosarum
title_short Light regulates attachment, exopolysaccharide production, and nodulation in Rhizobium leguminosarum through a LOV-histidine kinase photoreceptor
title_full Light regulates attachment, exopolysaccharide production, and nodulation in Rhizobium leguminosarum through a LOV-histidine kinase photoreceptor
title_fullStr Light regulates attachment, exopolysaccharide production, and nodulation in Rhizobium leguminosarum through a LOV-histidine kinase photoreceptor
title_full_unstemmed Light regulates attachment, exopolysaccharide production, and nodulation in Rhizobium leguminosarum through a LOV-histidine kinase photoreceptor
title_sort Light regulates attachment, exopolysaccharide production, and nodulation in Rhizobium leguminosarum through a LOV-histidine kinase photoreceptor
dc.creator.none.fl_str_mv Bonomi, H.R.
Posadas, D.M.
Paris, G.
Del Carmen Carrica, M.
Frederickson, M.
Pietrasanta, L.I.
Bogomolni, R.A.
Zorreguieta, A.
Goldbaum, F.A.
author Bonomi, H.R.
author_facet Bonomi, H.R.
Posadas, D.M.
Paris, G.
Del Carmen Carrica, M.
Frederickson, M.
Pietrasanta, L.I.
Bogomolni, R.A.
Zorreguieta, A.
Goldbaum, F.A.
author_role author
author2 Posadas, D.M.
Paris, G.
Del Carmen Carrica, M.
Frederickson, M.
Pietrasanta, L.I.
Bogomolni, R.A.
Zorreguieta, A.
Goldbaum, F.A.
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv bacterial polysaccharide
bacterial protein
exopolysaccharide
light oxygen and voltage histidine kinase
unclassified drug
adaptation
amino terminal sequence
article
bacterial gene
bacterium culture
biofilm
blue light
environmental factor
illumination
light
lov gene
nodulation
nonhuman
pea
plant root
priority journal
protein synthesis
real time polymerase chain reaction
reverse transcription polymerase chain reaction
Rhizobium leguminosarum
symbiosis
Amino Acid Sequence
Bacterial Adhesion
Base Sequence
Biofilms
Blotting, Western
Flagella
Gentian Violet
Light
Microscopy, Electron, Scanning
Molecular Sequence Data
Peas
Photoreceptors, Microbial
Plant Root Nodulation
Polysaccharides, Bacterial
Protein Kinases
Protein Structure, Tertiary
Real-Time Polymerase Chain Reaction
Rhizobium leguminosarum
Sequence Alignment
Sequence Analysis, DNA
Statistics, Nonparametric
Symbiosis
algae
Bacteria (microorganisms)
Embryophyta
Fabaceae
Fungi
Pisum sativum
Rhizobium leguminosarum
topic bacterial polysaccharide
bacterial protein
exopolysaccharide
light oxygen and voltage histidine kinase
unclassified drug
adaptation
amino terminal sequence
article
bacterial gene
bacterium culture
biofilm
blue light
environmental factor
illumination
light
lov gene
nodulation
nonhuman
pea
plant root
priority journal
protein synthesis
real time polymerase chain reaction
reverse transcription polymerase chain reaction
Rhizobium leguminosarum
symbiosis
Amino Acid Sequence
Bacterial Adhesion
Base Sequence
Biofilms
Blotting, Western
Flagella
Gentian Violet
Light
Microscopy, Electron, Scanning
Molecular Sequence Data
Peas
Photoreceptors, Microbial
Plant Root Nodulation
Polysaccharides, Bacterial
Protein Kinases
Protein Structure, Tertiary
Real-Time Polymerase Chain Reaction
Rhizobium leguminosarum
Sequence Alignment
Sequence Analysis, DNA
Statistics, Nonparametric
Symbiosis
algae
Bacteria (microorganisms)
Embryophyta
Fabaceae
Fungi
Pisum sativum
Rhizobium leguminosarum
dc.description.none.fl_txt_mv Rhizobium leguminosarum is a soil bacterium that infects root hairs and induces the formation of nitrogen-fixing nodules on leguminous plants. Light, oxygen, and voltage (LOV)-domain proteins are bluelight receptors found in higher plants and many algae, fungi, and bacteria. The genome of R. leguminosarum bv. viciae 3841, a peanodulating endosymbiont, encodes a sensor histidine kinase containing a LOV domain at the N-terminal end (R-LOV-HK). R-LOV-HK has a typical LOV domain absorption spectrum with broad bands in the blue and UV-A regions and shows a truncated photocycle. Here we show that the R-LOV-HK protein regulates attachment to an abiotic surface and production of flagellar proteins and exopolysaccharide in response to light. Also, illumination of bacterial cultures before inoculation of pea roots increases the number of nodules per plant and the number of intranodular bacteroids. The effects of light on nodulation are dependent on a functional lov gene. The results presented in this work suggest that light, sensed by R-LOV-HK, is an important environmental factor that controls adaptive responses and the symbiotic efficiency of R. leguminosarum.
Fil:Posadas, D.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Zorreguieta, A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
description Rhizobium leguminosarum is a soil bacterium that infects root hairs and induces the formation of nitrogen-fixing nodules on leguminous plants. Light, oxygen, and voltage (LOV)-domain proteins are bluelight receptors found in higher plants and many algae, fungi, and bacteria. The genome of R. leguminosarum bv. viciae 3841, a peanodulating endosymbiont, encodes a sensor histidine kinase containing a LOV domain at the N-terminal end (R-LOV-HK). R-LOV-HK has a typical LOV domain absorption spectrum with broad bands in the blue and UV-A regions and shows a truncated photocycle. Here we show that the R-LOV-HK protein regulates attachment to an abiotic surface and production of flagellar proteins and exopolysaccharide in response to light. Also, illumination of bacterial cultures before inoculation of pea roots increases the number of nodules per plant and the number of intranodular bacteroids. The effects of light on nodulation are dependent on a functional lov gene. The results presented in this work suggest that light, sensed by R-LOV-HK, is an important environmental factor that controls adaptive responses and the symbiotic efficiency of R. leguminosarum.
publishDate 2012
dc.date.none.fl_str_mv 2012
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/20.500.12110/paper_00278424_v109_n30_p12135_Bonomi
url http://hdl.handle.net/20.500.12110/paper_00278424_v109_n30_p12135_Bonomi
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/2.5/ar
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/2.5/ar
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv Proc. Natl. Acad. Sci. U. S. A. 2012;109(30):12135-12140
reponame:Biblioteca Digital (UBA-FCEN)
instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron:UBA-FCEN
reponame_str Biblioteca Digital (UBA-FCEN)
collection Biblioteca Digital (UBA-FCEN)
instname_str Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron_str UBA-FCEN
institution UBA-FCEN
repository.name.fl_str_mv Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
repository.mail.fl_str_mv ana@bl.fcen.uba.ar
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