BlsA is a low to moderate temperature blue light photoreceptor in the human pathogen acinetobacter baumannii
- Autores
- Golic, Adrián Ezequiel; Valle, Lorena; Jaime, Paula Constanza; Alvarez, Clarisa Ester; Parodi, Clarisa; Borsarelli, Claudio Darío; Abatedaga, Maria Ines de Los Angeles; Mussi, María Alejandra
- Año de publicación
- 2019
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Light is an environmental signal that produces extensive effects on the physiology of the human pathogen Acinetobacter baumannii. Many of the bacterial responses to light depend on BlsA, a bluelight using FAD (BLUF)-type photoreceptor, which also integrates temperature signals. In this work, we disclose novel mechanistic aspects of the function of BlsA. First, we show that light modulation of motility occurs only at temperatures lower than 24◦C, a phenotype depending on BlsA. Second, blsA transcript levels were significantly reduced at temperatures higher than 25◦C, in agreement with BlsA protein levels in the cell which were undetectable at 26◦C and higher temperatures. Also, quantum yield of photo-activation of BlsA (lBlsA) between 14 and 37◦C, showed that BlsA photoactivity is greatly compromised at 25◦C and absent above 28◦C. Fluorescence emission and anisotropy of the cofactor together with the intrinsic protein fluorescence studies suggest that the FAD binding site is more susceptible to structural changes caused by increments in temperature than other regions of the protein. Moreover, BlsA itself gains structural instability and strongly aggregates at temperatures above 30◦C. Overall, BlsA is a low to moderate temperature photoreceptor, whose functioning is highly regulated in the cell, with control points at expression of the cognate gene as well as photoactivity.
Fil: Golic, Adrián Ezequiel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; Argentina
Fil: Valle, Lorena. Universidad Nacional de Santiago del Estero. Instituto de Bionanotecnología del Noa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Bionanotecnología del Noa; Argentina
Fil: Jaime, Paula Constanza. Universidad Nacional de Santiago del Estero. Instituto de Bionanotecnología del Noa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Bionanotecnología del Noa; Argentina
Fil: Alvarez, Clarisa Ester. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; Argentina
Fil: Parodi, Clarisa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; Argentina
Fil: Borsarelli, Claudio Darío. Universidad Nacional de Santiago del Estero. Instituto de Bionanotecnología del Noa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Bionanotecnología del Noa; Argentina
Fil: Abatedaga, Maria Ines de Los Angeles. Universidad Nacional de Santiago del Estero. Instituto de Bionanotecnología del Noa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Bionanotecnología del Noa; Argentina
Fil: Mussi, María Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; Argentina - Materia
-
ACINETOBACTER BAUMANNII
BLUF
MOTILITY
PHOTOACTIVITY
TEMPERATURE MODULATION - 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:11336/180932
Ver los metadatos del registro completo
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oai:ri.conicet.gov.ar:11336/180932 |
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CONICET Digital (CONICET) |
spelling |
BlsA is a low to moderate temperature blue light photoreceptor in the human pathogen acinetobacter baumanniiGolic, Adrián EzequielValle, LorenaJaime, Paula ConstanzaAlvarez, Clarisa EsterParodi, ClarisaBorsarelli, Claudio DaríoAbatedaga, Maria Ines de Los AngelesMussi, María AlejandraACINETOBACTER BAUMANNIIBLUFMOTILITYPHOTOACTIVITYTEMPERATURE MODULATIONhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Light is an environmental signal that produces extensive effects on the physiology of the human pathogen Acinetobacter baumannii. Many of the bacterial responses to light depend on BlsA, a bluelight using FAD (BLUF)-type photoreceptor, which also integrates temperature signals. In this work, we disclose novel mechanistic aspects of the function of BlsA. First, we show that light modulation of motility occurs only at temperatures lower than 24◦C, a phenotype depending on BlsA. Second, blsA transcript levels were significantly reduced at temperatures higher than 25◦C, in agreement with BlsA protein levels in the cell which were undetectable at 26◦C and higher temperatures. Also, quantum yield of photo-activation of BlsA (lBlsA) between 14 and 37◦C, showed that BlsA photoactivity is greatly compromised at 25◦C and absent above 28◦C. Fluorescence emission and anisotropy of the cofactor together with the intrinsic protein fluorescence studies suggest that the FAD binding site is more susceptible to structural changes caused by increments in temperature than other regions of the protein. Moreover, BlsA itself gains structural instability and strongly aggregates at temperatures above 30◦C. Overall, BlsA is a low to moderate temperature photoreceptor, whose functioning is highly regulated in the cell, with control points at expression of the cognate gene as well as photoactivity.Fil: Golic, Adrián Ezequiel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; ArgentinaFil: Valle, Lorena. Universidad Nacional de Santiago del Estero. Instituto de Bionanotecnología del Noa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Bionanotecnología del Noa; ArgentinaFil: Jaime, Paula Constanza. Universidad Nacional de Santiago del Estero. Instituto de Bionanotecnología del Noa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Bionanotecnología del Noa; ArgentinaFil: Alvarez, Clarisa Ester. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; ArgentinaFil: Parodi, Clarisa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; ArgentinaFil: Borsarelli, Claudio Darío. Universidad Nacional de Santiago del Estero. Instituto de Bionanotecnología del Noa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Bionanotecnología del Noa; ArgentinaFil: Abatedaga, Maria Ines de Los Angeles. Universidad Nacional de Santiago del Estero. Instituto de Bionanotecnología del Noa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Bionanotecnología del Noa; ArgentinaFil: Mussi, María Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; ArgentinaFrontiers Media2019-08-21info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/180932Golic, Adrián Ezequiel; Valle, Lorena; Jaime, Paula Constanza; Alvarez, Clarisa Ester; Parodi, Clarisa; et al.; BlsA is a low to moderate temperature blue light photoreceptor in the human pathogen acinetobacter baumannii; Frontiers Media; Frontiers in Microbiology; 10; 21-8-2019; 1-111664-302XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.frontiersin.org/article/10.3389/fmicb.2019.01925/fullinfo:eu-repo/semantics/altIdentifier/doi/10.3389/fmicb.2019.01925info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T14:28:07Zoai:ri.conicet.gov.ar:11336/180932instacron: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:34982025-10-15 14:28:07.413CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
BlsA is a low to moderate temperature blue light photoreceptor in the human pathogen acinetobacter baumannii |
title |
BlsA is a low to moderate temperature blue light photoreceptor in the human pathogen acinetobacter baumannii |
spellingShingle |
BlsA is a low to moderate temperature blue light photoreceptor in the human pathogen acinetobacter baumannii Golic, Adrián Ezequiel ACINETOBACTER BAUMANNII BLUF MOTILITY PHOTOACTIVITY TEMPERATURE MODULATION |
title_short |
BlsA is a low to moderate temperature blue light photoreceptor in the human pathogen acinetobacter baumannii |
title_full |
BlsA is a low to moderate temperature blue light photoreceptor in the human pathogen acinetobacter baumannii |
title_fullStr |
BlsA is a low to moderate temperature blue light photoreceptor in the human pathogen acinetobacter baumannii |
title_full_unstemmed |
BlsA is a low to moderate temperature blue light photoreceptor in the human pathogen acinetobacter baumannii |
title_sort |
BlsA is a low to moderate temperature blue light photoreceptor in the human pathogen acinetobacter baumannii |
dc.creator.none.fl_str_mv |
Golic, Adrián Ezequiel Valle, Lorena Jaime, Paula Constanza Alvarez, Clarisa Ester Parodi, Clarisa Borsarelli, Claudio Darío Abatedaga, Maria Ines de Los Angeles Mussi, María Alejandra |
author |
Golic, Adrián Ezequiel |
author_facet |
Golic, Adrián Ezequiel Valle, Lorena Jaime, Paula Constanza Alvarez, Clarisa Ester Parodi, Clarisa Borsarelli, Claudio Darío Abatedaga, Maria Ines de Los Angeles Mussi, María Alejandra |
author_role |
author |
author2 |
Valle, Lorena Jaime, Paula Constanza Alvarez, Clarisa Ester Parodi, Clarisa Borsarelli, Claudio Darío Abatedaga, Maria Ines de Los Angeles Mussi, María Alejandra |
author2_role |
author author author author author author author |
dc.subject.none.fl_str_mv |
ACINETOBACTER BAUMANNII BLUF MOTILITY PHOTOACTIVITY TEMPERATURE MODULATION |
topic |
ACINETOBACTER BAUMANNII BLUF MOTILITY PHOTOACTIVITY TEMPERATURE MODULATION |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
Light is an environmental signal that produces extensive effects on the physiology of the human pathogen Acinetobacter baumannii. Many of the bacterial responses to light depend on BlsA, a bluelight using FAD (BLUF)-type photoreceptor, which also integrates temperature signals. In this work, we disclose novel mechanistic aspects of the function of BlsA. First, we show that light modulation of motility occurs only at temperatures lower than 24◦C, a phenotype depending on BlsA. Second, blsA transcript levels were significantly reduced at temperatures higher than 25◦C, in agreement with BlsA protein levels in the cell which were undetectable at 26◦C and higher temperatures. Also, quantum yield of photo-activation of BlsA (lBlsA) between 14 and 37◦C, showed that BlsA photoactivity is greatly compromised at 25◦C and absent above 28◦C. Fluorescence emission and anisotropy of the cofactor together with the intrinsic protein fluorescence studies suggest that the FAD binding site is more susceptible to structural changes caused by increments in temperature than other regions of the protein. Moreover, BlsA itself gains structural instability and strongly aggregates at temperatures above 30◦C. Overall, BlsA is a low to moderate temperature photoreceptor, whose functioning is highly regulated in the cell, with control points at expression of the cognate gene as well as photoactivity. Fil: Golic, Adrián Ezequiel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; Argentina Fil: Valle, Lorena. Universidad Nacional de Santiago del Estero. Instituto de Bionanotecnología del Noa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Bionanotecnología del Noa; Argentina Fil: Jaime, Paula Constanza. Universidad Nacional de Santiago del Estero. Instituto de Bionanotecnología del Noa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Bionanotecnología del Noa; Argentina Fil: Alvarez, Clarisa Ester. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; Argentina Fil: Parodi, Clarisa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; Argentina Fil: Borsarelli, Claudio Darío. Universidad Nacional de Santiago del Estero. Instituto de Bionanotecnología del Noa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Bionanotecnología del Noa; Argentina Fil: Abatedaga, Maria Ines de Los Angeles. Universidad Nacional de Santiago del Estero. Instituto de Bionanotecnología del Noa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Bionanotecnología del Noa; Argentina Fil: Mussi, María Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosintéticos y Bioquímicos. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; Argentina |
description |
Light is an environmental signal that produces extensive effects on the physiology of the human pathogen Acinetobacter baumannii. Many of the bacterial responses to light depend on BlsA, a bluelight using FAD (BLUF)-type photoreceptor, which also integrates temperature signals. In this work, we disclose novel mechanistic aspects of the function of BlsA. First, we show that light modulation of motility occurs only at temperatures lower than 24◦C, a phenotype depending on BlsA. Second, blsA transcript levels were significantly reduced at temperatures higher than 25◦C, in agreement with BlsA protein levels in the cell which were undetectable at 26◦C and higher temperatures. Also, quantum yield of photo-activation of BlsA (lBlsA) between 14 and 37◦C, showed that BlsA photoactivity is greatly compromised at 25◦C and absent above 28◦C. Fluorescence emission and anisotropy of the cofactor together with the intrinsic protein fluorescence studies suggest that the FAD binding site is more susceptible to structural changes caused by increments in temperature than other regions of the protein. Moreover, BlsA itself gains structural instability and strongly aggregates at temperatures above 30◦C. Overall, BlsA is a low to moderate temperature photoreceptor, whose functioning is highly regulated in the cell, with control points at expression of the cognate gene as well as photoactivity. |
publishDate |
2019 |
dc.date.none.fl_str_mv |
2019-08-21 |
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/11336/180932 Golic, Adrián Ezequiel; Valle, Lorena; Jaime, Paula Constanza; Alvarez, Clarisa Ester; Parodi, Clarisa; et al.; BlsA is a low to moderate temperature blue light photoreceptor in the human pathogen acinetobacter baumannii; Frontiers Media; Frontiers in Microbiology; 10; 21-8-2019; 1-11 1664-302X CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/180932 |
identifier_str_mv |
Golic, Adrián Ezequiel; Valle, Lorena; Jaime, Paula Constanza; Alvarez, Clarisa Ester; Parodi, Clarisa; et al.; BlsA is a low to moderate temperature blue light photoreceptor in the human pathogen acinetobacter baumannii; Frontiers Media; Frontiers in Microbiology; 10; 21-8-2019; 1-11 1664-302X 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/article/10.3389/fmicb.2019.01925/full info:eu-repo/semantics/altIdentifier/doi/10.3389/fmicb.2019.01925 |
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 |
Frontiers Media |
publisher.none.fl_str_mv |
Frontiers Media |
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_ |
1846082743143759872 |
score |
13.22299 |