Mostrar el registro sencillo del ítem
dc.contributor.author
Albarracín, Virginia Helena
dc.contributor.author
Simon, Julian
dc.contributor.author
Pathak, Gopal P.
dc.contributor.author
Valle, Lorena
dc.contributor.author
Douki, Thierry
dc.contributor.author
Cadet, Jean
dc.contributor.author
Borsarelli, Claudio Darío
dc.contributor.author
Farias, Maria Eugenia
dc.contributor.author
Gärtner, Wolfgang
dc.date.available
2017-11-13T16:45:57Z
dc.date.issued
2014-05
dc.identifier.citation
Albarracín, Virginia Helena; Simon, Julian; Pathak, Gopal P.; Valle, Lorena; Douki, Thierry; et al.; First characterisation of a CPD-class I photolyase from a UV-resistant extremophile isolated from High-Altitude Andean Lakes; Royal Society of Chemistry; Photochemical and Photobiological Sciences; 13; 5; 5-2014; 739-750
dc.identifier.issn
1474-905X
dc.identifier.uri
http://hdl.handle.net/11336/28018
dc.description.abstract
UV-resistant Acinetobacter sp. Ver3 isolated from High-Altitude Andean Lakes (HAAL) in Argentinean Puna, one of the highest UV exposed ecosystems on Earth, showed efficient DNA photorepairing ability, coupled to highly efficient antioxidant enzyme activities in response to UV-B stress. We herein present the cloning, expression, and functional characterization of a cyclobutane pyrimidine dimer (CPD)-class I photolyase (Ver3Phr) from this extremophile to prove its involvement in the previously noted survival capability. Spectroscopy of the overexpressed and purified protein identified flavin adenine dinucleotide (FAD) and 5,10-methenyltetrahydrofolate (MTHF) as chromophore and antenna molecules, respectively. All functional analyses were performed in parallel with the ortholog E. coli photolyase. Whereas the E. coli enzyme showed the FAD chromophore as a mixture of oxidised and reduced states, the Ver3 chromophore always remained partly (including the semiquinone state) or fully reduced under all experimental conditions tested. Functional complementation of Ver3Phr in Phr−-RecA E. coli strains was assessed by traditional UFC counting and measurement of DNA bipyrimidine photoproducts by HPLC coupled with electrospray ionisation-tandem mass spectrometry (ESI-MS/MS) detection. The results identified strong photoreactivation ability in vivo of Ver3Phr while its nonphotoreactivation function, probably related with the stimulation of nucleotide excision repair (NER), was not as manifest as for EcPhr. Whether this is a question of the approach using an exogenous photolyase incorporated in a non-genuine host or a fundamental different behaviour of a novel enzyme from an exotic environment will need further studies.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Royal Society of Chemistry
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Acinetobacter
dc.subject
Extremophiles
dc.subject
High-Altitude Andean Lakes
dc.subject
Photolyase
dc.subject.classification
Otras Ciencias Biológicas
dc.subject.classification
Ciencias Biológicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
First characterisation of a CPD-class I photolyase from a UV-resistant extremophile isolated from High-Altitude Andean Lakes
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2017-10-31T17:50:12Z
dc.journal.volume
13
dc.journal.number
5
dc.journal.pagination
739-750
dc.journal.pais
Reino Unido
dc.journal.ciudad
Cambridge
dc.description.fil
Fil: Albarracín, Virginia Helena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Planta Piloto de Procesos Industriales Microbiologicos; Argentina. Universidad Nacional de Tucumán. Facultad de Ciencias Naturales e Instituto Miguel Lillo; Argentina. Max Planck Institute for Chemical Energy Conversion; Alemania
dc.description.fil
Fil: Simon, Julian. Max Planck Institute for Chemical Energy Conversion; Alemania
dc.description.fil
Fil: Pathak, Gopal P.. Max Planck Institute for Chemical Energy Conversion; Alemania
dc.description.fil
Fil: Valle, Lorena. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero. Universidad Nacional de Santiago del Estero. Centro de Investigaciones y Transferencia de Santiago del Estero; Argentina
dc.description.fil
Fil: Douki, Thierry. Laboratoire “Lésions des Acides Nucléiques”; Francia
dc.description.fil
Fil: Cadet, Jean. Laboratoire “Lésions des Acides Nucléiques”; Francia
dc.description.fil
Fil: Borsarelli, Claudio Darío. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero. Universidad Nacional de Santiago del Estero. Centro de Investigaciones y Transferencia de Santiago del Estero; Argentina
dc.description.fil
Fil: Farias, Maria Eugenia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Planta Piloto de Procesos Industriales Microbiologicos; Argentina
dc.description.fil
Fil: Gärtner, Wolfgang. Max Planck Institute for Chemical Energy Conversion; Alemania
dc.journal.title
Photochemical and Photobiological Sciences
dc.relation.isreferencedin
info:eu-repo/semantics/reference/url/http://pubs.rsc.org/-/content/articlelanding/2014/pp/c3pp50399b#!divAbstract
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/https://dx.doi.org/10.1039/C3PP50399B
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://pubs.rsc.org/-/content/articlelanding/2014/pp/c3pp50399b#!divAbstract
Archivos asociados