UV Resistance and Photoreactivation of Extremophiles from High-Altitude Andean Lakes

Autores
Albarracín, Virginia Helena; Gärtner, Wolfang; Farias, Maria Eugenia
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
He HAAL are natural laboratories for exploring and monitoring in situ interactions between the geophysical environment and the dynamics of biodiversity. Solar irradiation (including high UV-B doses) is without doubt the factor that puts the greatest pressure on the ecology of the microbial communities thriving in these shallow lakes. Thus, it is not surprising that ~100 strains with intrinsic UV-B-resistance have been isolated from HAAL. These organisms have developed strategies to cope with strong UV-B irradiation to avoid severe UV-B-damage to proteins, lipids and DNA. Hence, microbiota at the HAAL may harbor special mechanisms to sense and respond to such a ubiquitous resource, i.e., light. In accordance with this, we have encountered a rich diversity of photoreceptors within the cryptochrome-photolyase family in the genomes of three UV-B-resistant extremophiles. Of particular importance among these photoreceptors was the finding of a photolyase-coding sequence in the genome of Acinetobacter sp. Ver3 strain that displayed efficient photoreactivation ability after strong UV-B-induced DNA damage. Based on sequence alignments and secondary structure predictions for this novel photolyase, and entries in the PDB, we found the highest three-dimensional similarity to the photolyase from E. coli (PDB 1DNPA). The structure revealed a proximal alpha-beta domain, and a distal helical domain that binds to FAD in full accordance to the structure of the E. coli photolyase. The N-terminal anti-parallel bundle of beta sheets enclosed by alpha helices is a typical folding motif of photolyases. The chain of three-tryptophan residues instrumental for electron transfer reaction is also conserved in Ver3 photolyase, and in close proximity to the isoalloxazine ring of FAD. All the former findings support the putative CPD-photolyase property of this protein, and agree with the efficient ability of Ver3 for repairing CPD lesions. Nevertheless, a more detailed functional characterization of this "extremoenzyme" is being conducted at the moment to clarify its repair function. The scenario pictured herein makes the HAAL microorganisms excellent test cases for exploring novel enzymatic functions driven by light, and for the bioprospection of novel molecules with potential biotechnological applications on energy conversion, biomedicine or industry. This brief overview is intended to "shine" scientific light on a high window from a quite unexplored, exotic environment, which otherwise constitutes an exceptional outdoor photobiology lab.
Fil: Albarracín, Virginia Helena. Universidad Nacional de Tucumán. Facultad de Ciencias Naturales e Instituto Miguel Lillo; Argentina. Max Planck Institute for Chemical Energy Conversion; Alemania. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; Argentina
Fil: Gärtner, Wolfang. Max Planck Institute for Chemical Energy Conversion; Alemania
Fil: Farias, Maria Eugenia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; Argentina
Materia
Uv Resistance
Anden Lakes
Extremophiles
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:11336/1765

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spelling UV Resistance and Photoreactivation of Extremophiles from High-Altitude Andean LakesAlbarracín, Virginia HelenaGärtner, WolfangFarias, Maria EugeniaUv ResistanceAnden LakesExtremophileshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1He HAAL are natural laboratories for exploring and monitoring in situ interactions between the geophysical environment and the dynamics of biodiversity. Solar irradiation (including high UV-B doses) is without doubt the factor that puts the greatest pressure on the ecology of the microbial communities thriving in these shallow lakes. Thus, it is not surprising that ~100 strains with intrinsic UV-B-resistance have been isolated from HAAL. These organisms have developed strategies to cope with strong UV-B irradiation to avoid severe UV-B-damage to proteins, lipids and DNA. Hence, microbiota at the HAAL may harbor special mechanisms to sense and respond to such a ubiquitous resource, i.e., light. In accordance with this, we have encountered a rich diversity of photoreceptors within the cryptochrome-photolyase family in the genomes of three UV-B-resistant extremophiles. Of particular importance among these photoreceptors was the finding of a photolyase-coding sequence in the genome of Acinetobacter sp. Ver3 strain that displayed efficient photoreactivation ability after strong UV-B-induced DNA damage. Based on sequence alignments and secondary structure predictions for this novel photolyase, and entries in the PDB, we found the highest three-dimensional similarity to the photolyase from E. coli (PDB 1DNPA). The structure revealed a proximal alpha-beta domain, and a distal helical domain that binds to FAD in full accordance to the structure of the E. coli photolyase. The N-terminal anti-parallel bundle of beta sheets enclosed by alpha helices is a typical folding motif of photolyases. The chain of three-tryptophan residues instrumental for electron transfer reaction is also conserved in Ver3 photolyase, and in close proximity to the isoalloxazine ring of FAD. All the former findings support the putative CPD-photolyase property of this protein, and agree with the efficient ability of Ver3 for repairing CPD lesions. Nevertheless, a more detailed functional characterization of this "extremoenzyme" is being conducted at the moment to clarify its repair function. The scenario pictured herein makes the HAAL microorganisms excellent test cases for exploring novel enzymatic functions driven by light, and for the bioprospection of novel molecules with potential biotechnological applications on energy conversion, biomedicine or industry. This brief overview is intended to "shine" scientific light on a high window from a quite unexplored, exotic environment, which otherwise constitutes an exceptional outdoor photobiology lab.Fil: Albarracín, Virginia Helena. Universidad Nacional de Tucumán. Facultad de Ciencias Naturales e Instituto Miguel Lillo; Argentina. Max Planck Institute for Chemical Energy Conversion; Alemania. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; ArgentinaFil: Gärtner, Wolfang. Max Planck Institute for Chemical Energy Conversion; AlemaniaFil: Farias, Maria Eugenia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; ArgentinaElsevier2013-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/1765Albarracín, Virginia Helena; Gärtner, Wolfang; Farias, Maria Eugenia; UV Resistance and Photoreactivation of Extremophiles from High-Altitude Andean Lakes; Elsevier; Journal of Photochemistry and Photobiology B: Biology; 4-2013; 1-41011-1344enginfo:eu-repo/semantics/altIdentifier/url/http://www.photobiology.info/Albarracin.htmlinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:37:36Zoai:ri.conicet.gov.ar:11336/1765instacron: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 09:37:36.93CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv UV Resistance and Photoreactivation of Extremophiles from High-Altitude Andean Lakes
title UV Resistance and Photoreactivation of Extremophiles from High-Altitude Andean Lakes
spellingShingle UV Resistance and Photoreactivation of Extremophiles from High-Altitude Andean Lakes
Albarracín, Virginia Helena
Uv Resistance
Anden Lakes
Extremophiles
title_short UV Resistance and Photoreactivation of Extremophiles from High-Altitude Andean Lakes
title_full UV Resistance and Photoreactivation of Extremophiles from High-Altitude Andean Lakes
title_fullStr UV Resistance and Photoreactivation of Extremophiles from High-Altitude Andean Lakes
title_full_unstemmed UV Resistance and Photoreactivation of Extremophiles from High-Altitude Andean Lakes
title_sort UV Resistance and Photoreactivation of Extremophiles from High-Altitude Andean Lakes
dc.creator.none.fl_str_mv Albarracín, Virginia Helena
Gärtner, Wolfang
Farias, Maria Eugenia
author Albarracín, Virginia Helena
author_facet Albarracín, Virginia Helena
Gärtner, Wolfang
Farias, Maria Eugenia
author_role author
author2 Gärtner, Wolfang
Farias, Maria Eugenia
author2_role author
author
dc.subject.none.fl_str_mv Uv Resistance
Anden Lakes
Extremophiles
topic Uv Resistance
Anden Lakes
Extremophiles
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv He HAAL are natural laboratories for exploring and monitoring in situ interactions between the geophysical environment and the dynamics of biodiversity. Solar irradiation (including high UV-B doses) is without doubt the factor that puts the greatest pressure on the ecology of the microbial communities thriving in these shallow lakes. Thus, it is not surprising that ~100 strains with intrinsic UV-B-resistance have been isolated from HAAL. These organisms have developed strategies to cope with strong UV-B irradiation to avoid severe UV-B-damage to proteins, lipids and DNA. Hence, microbiota at the HAAL may harbor special mechanisms to sense and respond to such a ubiquitous resource, i.e., light. In accordance with this, we have encountered a rich diversity of photoreceptors within the cryptochrome-photolyase family in the genomes of three UV-B-resistant extremophiles. Of particular importance among these photoreceptors was the finding of a photolyase-coding sequence in the genome of Acinetobacter sp. Ver3 strain that displayed efficient photoreactivation ability after strong UV-B-induced DNA damage. Based on sequence alignments and secondary structure predictions for this novel photolyase, and entries in the PDB, we found the highest three-dimensional similarity to the photolyase from E. coli (PDB 1DNPA). The structure revealed a proximal alpha-beta domain, and a distal helical domain that binds to FAD in full accordance to the structure of the E. coli photolyase. The N-terminal anti-parallel bundle of beta sheets enclosed by alpha helices is a typical folding motif of photolyases. The chain of three-tryptophan residues instrumental for electron transfer reaction is also conserved in Ver3 photolyase, and in close proximity to the isoalloxazine ring of FAD. All the former findings support the putative CPD-photolyase property of this protein, and agree with the efficient ability of Ver3 for repairing CPD lesions. Nevertheless, a more detailed functional characterization of this "extremoenzyme" is being conducted at the moment to clarify its repair function. The scenario pictured herein makes the HAAL microorganisms excellent test cases for exploring novel enzymatic functions driven by light, and for the bioprospection of novel molecules with potential biotechnological applications on energy conversion, biomedicine or industry. This brief overview is intended to "shine" scientific light on a high window from a quite unexplored, exotic environment, which otherwise constitutes an exceptional outdoor photobiology lab.
Fil: Albarracín, Virginia Helena. Universidad Nacional de Tucumán. Facultad de Ciencias Naturales e Instituto Miguel Lillo; Argentina. Max Planck Institute for Chemical Energy Conversion; Alemania. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; Argentina
Fil: Gärtner, Wolfang. Max Planck Institute for Chemical Energy Conversion; Alemania
Fil: Farias, Maria Eugenia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; Argentina
description He HAAL are natural laboratories for exploring and monitoring in situ interactions between the geophysical environment and the dynamics of biodiversity. Solar irradiation (including high UV-B doses) is without doubt the factor that puts the greatest pressure on the ecology of the microbial communities thriving in these shallow lakes. Thus, it is not surprising that ~100 strains with intrinsic UV-B-resistance have been isolated from HAAL. These organisms have developed strategies to cope with strong UV-B irradiation to avoid severe UV-B-damage to proteins, lipids and DNA. Hence, microbiota at the HAAL may harbor special mechanisms to sense and respond to such a ubiquitous resource, i.e., light. In accordance with this, we have encountered a rich diversity of photoreceptors within the cryptochrome-photolyase family in the genomes of three UV-B-resistant extremophiles. Of particular importance among these photoreceptors was the finding of a photolyase-coding sequence in the genome of Acinetobacter sp. Ver3 strain that displayed efficient photoreactivation ability after strong UV-B-induced DNA damage. Based on sequence alignments and secondary structure predictions for this novel photolyase, and entries in the PDB, we found the highest three-dimensional similarity to the photolyase from E. coli (PDB 1DNPA). The structure revealed a proximal alpha-beta domain, and a distal helical domain that binds to FAD in full accordance to the structure of the E. coli photolyase. The N-terminal anti-parallel bundle of beta sheets enclosed by alpha helices is a typical folding motif of photolyases. The chain of three-tryptophan residues instrumental for electron transfer reaction is also conserved in Ver3 photolyase, and in close proximity to the isoalloxazine ring of FAD. All the former findings support the putative CPD-photolyase property of this protein, and agree with the efficient ability of Ver3 for repairing CPD lesions. Nevertheless, a more detailed functional characterization of this "extremoenzyme" is being conducted at the moment to clarify its repair function. The scenario pictured herein makes the HAAL microorganisms excellent test cases for exploring novel enzymatic functions driven by light, and for the bioprospection of novel molecules with potential biotechnological applications on energy conversion, biomedicine or industry. This brief overview is intended to "shine" scientific light on a high window from a quite unexplored, exotic environment, which otherwise constitutes an exceptional outdoor photobiology lab.
publishDate 2013
dc.date.none.fl_str_mv 2013-04
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/11336/1765
Albarracín, Virginia Helena; Gärtner, Wolfang; Farias, Maria Eugenia; UV Resistance and Photoreactivation of Extremophiles from High-Altitude Andean Lakes; Elsevier; Journal of Photochemistry and Photobiology B: Biology; 4-2013; 1-4
1011-1344
url http://hdl.handle.net/11336/1765
identifier_str_mv Albarracín, Virginia Helena; Gärtner, Wolfang; Farias, Maria Eugenia; UV Resistance and Photoreactivation of Extremophiles from High-Altitude Andean Lakes; Elsevier; Journal of Photochemistry and Photobiology B: Biology; 4-2013; 1-4
1011-1344
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.photobiology.info/Albarracin.html
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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 Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
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reponame_str CONICET Digital (CONICET)
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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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