A study on Pr-induced variants of XccBphP bacteriophytochrome photoreceptor from Xanthomonas campestris

Autores
Conforte, Valeria Paola; Otero, Lisandro Horacio; Toum, Laila; Antelo, Giuliano Tomás; Rinaldi, Jimena Julieta; Klinke, Sebastian; Sirigu, Serena; Chavas, Leonardo; Vojnov, Adrián Alberto; Goldbaum, Fernando Alberto; Malamud, Florencia; Bonomi, Hernán Ruy
Año de publicación
2020
Idioma
inglés
Tipo de recurso
documento de conferencia
Estado
versión publicada
Descripción
Red and far-red light sensing bacteriophytochrome photoreceptor (BphP) and blue light sensing LOV domain proteins have been showed to play key roles in bacterial physiology and in virulence factors (VFs) modulation. We have previously shown that Xanthomonas campestris pv. campestris (Xcc), the causal agent of black rot disease, has in its genome a sequence that encodes for a single bathy type BphP (XccBphP) that negatively regulates its virulence. These bilin-binding proteins have the capacity to photoswitch between two states, Pr (redabsorbing) and Pfr (far-red absorbing), by the isomerization of the bilin chromophore and generating structural changes that result inthe transduction of the light signal into biochemical signaling. Here, we designed and constructed three different site-directed mutations that affect XccBphP photocycle favoring its Pr state: D199A, L193Q and L193N. The mutant recombinant proteins have beenproduced in vitro and assayed by UV-Vis spectroscopy, showing that Pris their preferred state. As expected, D199A locked the photoreceptor in a Pr-like state, however, L193Q and L193N transformed XccBphP froma bathy-type phytochrome into a canonical one, exhibiting a Pr thermal ground state. The X-ray structures for all the mutants were obtained in the Pr conformation, identical to the one from the wild-type previously determined, showing no significant differences in the quaternary, tertiary or secondary structures. Finally, wetested the in vivo implications of manipulating the XccBphPphotocycle using xanthan production and stomata aperture as thebiological responses of its signaling output. The null mutant complementation experiments show that locking XccBphP in a Pr-likestate (using D199A) or, converting it into a Pr-stabilized phytochrome (using L193N or L193Q) decreases bacterial exopolysaccharide production in dark condition when compared to null mutant. This is reverted when the complemented strains were grown under red light.
Fil: Conforte, Valeria Paola. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Ciencia y Tecnología "Dr. César Milstein". Fundación Pablo Cassará. Instituto de Ciencia y Tecnología "Dr. César Milstein"; Argentina
Fil: Otero, Lisandro Horacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina. Plataforma Argentina de Biología Estructural y Metabolómica; Argentina
Fil: Toum, Laila. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Ciencia y Tecnología "Dr. César Milstein". Fundación Pablo Cassará. Instituto de Ciencia y Tecnología "Dr. César Milstein"; Argentina
Fil: Antelo, Giuliano Tomás. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Rinaldi, Jimena Julieta. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Klinke, Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Sirigu, Serena. Synchrotron Soleil; Francia
Fil: Chavas, Leonardo. Synchrotron Soleil; Francia
Fil: Vojnov, Adrián Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Ciencia y Tecnología "Dr. César Milstein". Fundación Pablo Cassará. Instituto de Ciencia y Tecnología "Dr. César Milstein"; Argentina
Fil: Goldbaum, Fernando Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Fundación Instituto Leloir; Argentina
Fil: Malamud, Florencia. Universidad Nacional de Luján. Departamento de Ciencias Básicas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Bonomi, Hernán Ruy. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
V Reunión Grupo Argentino de Fotobiología
La Plata
Argentina
Grupo Argentino de Fotobiologia
Materia
SIGNAL TRANSDUCTION
RED-LIGHT PHOTORECEPTOR
X-RAY CRYSTALLOGRAPHY
XANTHAN PRODUCTION
STOMATA APERTURE
PHOTOBIOLOGICAL RESPONSES
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:11336/154747
Acceder
id CONICETDig_d36a20e74e41750efe114913f951dd30
oai_identifier_str oai:ri.conicet.gov.ar:11336/154747
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling A study on Pr-induced variants of XccBphP bacteriophytochrome photoreceptor from Xanthomonas campestrisConforte, Valeria PaolaOtero, Lisandro HoracioToum, LailaAntelo, Giuliano TomásRinaldi, Jimena JulietaKlinke, SebastianSirigu, SerenaChavas, LeonardoVojnov, Adrián AlbertoGoldbaum, Fernando AlbertoMalamud, FlorenciaBonomi, Hernán RuySIGNAL TRANSDUCTIONRED-LIGHT PHOTORECEPTORX-RAY CRYSTALLOGRAPHYXANTHAN PRODUCTIONSTOMATA APERTUREPHOTOBIOLOGICAL RESPONSEShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Red and far-red light sensing bacteriophytochrome photoreceptor (BphP) and blue light sensing LOV domain proteins have been showed to play key roles in bacterial physiology and in virulence factors (VFs) modulation. We have previously shown that Xanthomonas campestris pv. campestris (Xcc), the causal agent of black rot disease, has in its genome a sequence that encodes for a single bathy type BphP (XccBphP) that negatively regulates its virulence. These bilin-binding proteins have the capacity to photoswitch between two states, Pr (redabsorbing) and Pfr (far-red absorbing), by the isomerization of the bilin chromophore and generating structural changes that result inthe transduction of the light signal into biochemical signaling. Here, we designed and constructed three different site-directed mutations that affect XccBphP photocycle favoring its Pr state: D199A, L193Q and L193N. The mutant recombinant proteins have beenproduced in vitro and assayed by UV-Vis spectroscopy, showing that Pris their preferred state. As expected, D199A locked the photoreceptor in a Pr-like state, however, L193Q and L193N transformed XccBphP froma bathy-type phytochrome into a canonical one, exhibiting a Pr thermal ground state. The X-ray structures for all the mutants were obtained in the Pr conformation, identical to the one from the wild-type previously determined, showing no significant differences in the quaternary, tertiary or secondary structures. Finally, wetested the in vivo implications of manipulating the XccBphPphotocycle using xanthan production and stomata aperture as thebiological responses of its signaling output. The null mutant complementation experiments show that locking XccBphP in a Pr-likestate (using D199A) or, converting it into a Pr-stabilized phytochrome (using L193N or L193Q) decreases bacterial exopolysaccharide production in dark condition when compared to null mutant. This is reverted when the complemented strains were grown under red light.Fil: Conforte, Valeria Paola. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Ciencia y Tecnología "Dr. César Milstein". Fundación Pablo Cassará. Instituto de Ciencia y Tecnología "Dr. César Milstein"; ArgentinaFil: Otero, Lisandro Horacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina. Plataforma Argentina de Biología Estructural y Metabolómica; ArgentinaFil: Toum, Laila. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Ciencia y Tecnología "Dr. César Milstein". Fundación Pablo Cassará. Instituto de Ciencia y Tecnología "Dr. César Milstein"; ArgentinaFil: Antelo, Giuliano Tomás. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; ArgentinaFil: Rinaldi, Jimena Julieta. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; ArgentinaFil: Klinke, Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; ArgentinaFil: Sirigu, Serena. Synchrotron Soleil; FranciaFil: Chavas, Leonardo. Synchrotron Soleil; FranciaFil: Vojnov, Adrián Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Ciencia y Tecnología "Dr. César Milstein". Fundación Pablo Cassará. Instituto de Ciencia y Tecnología "Dr. César Milstein"; ArgentinaFil: Goldbaum, Fernando Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Fundación Instituto Leloir; ArgentinaFil: Malamud, Florencia. Universidad Nacional de Luján. Departamento de Ciencias Básicas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Bonomi, Hernán Ruy. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; ArgentinaV Reunión Grupo Argentino de FotobiologíaLa PlataArgentinaGrupo Argentino de FotobiologiaGrupo Argentino de Fotobiología2020info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/conferenceObjectReuniónBookhttp://purl.org/coar/resource_type/c_5794info:ar-repo/semantics/documentoDeConferenciaapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/154747A study on Pr-induced variants of XccBphP bacteriophytochrome photoreceptor from Xanthomonas campestris; V Reunión Grupo Argentino de Fotobiología; La Plata; Argentina; 2020; 1-11CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://grupoargentinodefotobiologia.info/site/site/grupar/pluginfile.php/94/mod_page/content/98/VGRAFOBLibroderesumenes.pdfinfo:eu-repo/semantics/altIdentifier/url/https://grupoargentinodefotobiologia.info/site/site/grupar/mod/page/view.php?id=14Nacionalinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T14:49:58Zoai:ri.conicet.gov.ar:11336/154747instacron: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 14:49:58.376CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv A study on Pr-induced variants of XccBphP bacteriophytochrome photoreceptor from Xanthomonas campestris
title A study on Pr-induced variants of XccBphP bacteriophytochrome photoreceptor from Xanthomonas campestris
spellingShingle A study on Pr-induced variants of XccBphP bacteriophytochrome photoreceptor from Xanthomonas campestris
Conforte, Valeria Paola
SIGNAL TRANSDUCTION
RED-LIGHT PHOTORECEPTOR
X-RAY CRYSTALLOGRAPHY
XANTHAN PRODUCTION
STOMATA APERTURE
PHOTOBIOLOGICAL RESPONSES
title_short A study on Pr-induced variants of XccBphP bacteriophytochrome photoreceptor from Xanthomonas campestris
title_full A study on Pr-induced variants of XccBphP bacteriophytochrome photoreceptor from Xanthomonas campestris
title_fullStr A study on Pr-induced variants of XccBphP bacteriophytochrome photoreceptor from Xanthomonas campestris
title_full_unstemmed A study on Pr-induced variants of XccBphP bacteriophytochrome photoreceptor from Xanthomonas campestris
title_sort A study on Pr-induced variants of XccBphP bacteriophytochrome photoreceptor from Xanthomonas campestris
dc.creator.none.fl_str_mv Conforte, Valeria Paola
Otero, Lisandro Horacio
Toum, Laila
Antelo, Giuliano Tomás
Rinaldi, Jimena Julieta
Klinke, Sebastian
Sirigu, Serena
Chavas, Leonardo
Vojnov, Adrián Alberto
Goldbaum, Fernando Alberto
Malamud, Florencia
Bonomi, Hernán Ruy
author Conforte, Valeria Paola
author_facet Conforte, Valeria Paola
Otero, Lisandro Horacio
Toum, Laila
Antelo, Giuliano Tomás
Rinaldi, Jimena Julieta
Klinke, Sebastian
Sirigu, Serena
Chavas, Leonardo
Vojnov, Adrián Alberto
Goldbaum, Fernando Alberto
Malamud, Florencia
Bonomi, Hernán Ruy
author_role author
author2 Otero, Lisandro Horacio
Toum, Laila
Antelo, Giuliano Tomás
Rinaldi, Jimena Julieta
Klinke, Sebastian
Sirigu, Serena
Chavas, Leonardo
Vojnov, Adrián Alberto
Goldbaum, Fernando Alberto
Malamud, Florencia
Bonomi, Hernán Ruy
author2_role author
author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv SIGNAL TRANSDUCTION
RED-LIGHT PHOTORECEPTOR
X-RAY CRYSTALLOGRAPHY
XANTHAN PRODUCTION
STOMATA APERTURE
PHOTOBIOLOGICAL RESPONSES
topic SIGNAL TRANSDUCTION
RED-LIGHT PHOTORECEPTOR
X-RAY CRYSTALLOGRAPHY
XANTHAN PRODUCTION
STOMATA APERTURE
PHOTOBIOLOGICAL RESPONSES
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Red and far-red light sensing bacteriophytochrome photoreceptor (BphP) and blue light sensing LOV domain proteins have been showed to play key roles in bacterial physiology and in virulence factors (VFs) modulation. We have previously shown that Xanthomonas campestris pv. campestris (Xcc), the causal agent of black rot disease, has in its genome a sequence that encodes for a single bathy type BphP (XccBphP) that negatively regulates its virulence. These bilin-binding proteins have the capacity to photoswitch between two states, Pr (redabsorbing) and Pfr (far-red absorbing), by the isomerization of the bilin chromophore and generating structural changes that result inthe transduction of the light signal into biochemical signaling. Here, we designed and constructed three different site-directed mutations that affect XccBphP photocycle favoring its Pr state: D199A, L193Q and L193N. The mutant recombinant proteins have beenproduced in vitro and assayed by UV-Vis spectroscopy, showing that Pris their preferred state. As expected, D199A locked the photoreceptor in a Pr-like state, however, L193Q and L193N transformed XccBphP froma bathy-type phytochrome into a canonical one, exhibiting a Pr thermal ground state. The X-ray structures for all the mutants were obtained in the Pr conformation, identical to the one from the wild-type previously determined, showing no significant differences in the quaternary, tertiary or secondary structures. Finally, wetested the in vivo implications of manipulating the XccBphPphotocycle using xanthan production and stomata aperture as thebiological responses of its signaling output. The null mutant complementation experiments show that locking XccBphP in a Pr-likestate (using D199A) or, converting it into a Pr-stabilized phytochrome (using L193N or L193Q) decreases bacterial exopolysaccharide production in dark condition when compared to null mutant. This is reverted when the complemented strains were grown under red light.
Fil: Conforte, Valeria Paola. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Ciencia y Tecnología "Dr. César Milstein". Fundación Pablo Cassará. Instituto de Ciencia y Tecnología "Dr. César Milstein"; Argentina
Fil: Otero, Lisandro Horacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina. Plataforma Argentina de Biología Estructural y Metabolómica; Argentina
Fil: Toum, Laila. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Ciencia y Tecnología "Dr. César Milstein". Fundación Pablo Cassará. Instituto de Ciencia y Tecnología "Dr. César Milstein"; Argentina
Fil: Antelo, Giuliano Tomás. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Rinaldi, Jimena Julieta. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Klinke, Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Sirigu, Serena. Synchrotron Soleil; Francia
Fil: Chavas, Leonardo. Synchrotron Soleil; Francia
Fil: Vojnov, Adrián Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Ciencia y Tecnología "Dr. César Milstein". Fundación Pablo Cassará. Instituto de Ciencia y Tecnología "Dr. César Milstein"; Argentina
Fil: Goldbaum, Fernando Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Fundación Instituto Leloir; Argentina
Fil: Malamud, Florencia. Universidad Nacional de Luján. Departamento de Ciencias Básicas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Bonomi, Hernán Ruy. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
V Reunión Grupo Argentino de Fotobiología
La Plata
Argentina
Grupo Argentino de Fotobiologia
description Red and far-red light sensing bacteriophytochrome photoreceptor (BphP) and blue light sensing LOV domain proteins have been showed to play key roles in bacterial physiology and in virulence factors (VFs) modulation. We have previously shown that Xanthomonas campestris pv. campestris (Xcc), the causal agent of black rot disease, has in its genome a sequence that encodes for a single bathy type BphP (XccBphP) that negatively regulates its virulence. These bilin-binding proteins have the capacity to photoswitch between two states, Pr (redabsorbing) and Pfr (far-red absorbing), by the isomerization of the bilin chromophore and generating structural changes that result inthe transduction of the light signal into biochemical signaling. Here, we designed and constructed three different site-directed mutations that affect XccBphP photocycle favoring its Pr state: D199A, L193Q and L193N. The mutant recombinant proteins have beenproduced in vitro and assayed by UV-Vis spectroscopy, showing that Pris their preferred state. As expected, D199A locked the photoreceptor in a Pr-like state, however, L193Q and L193N transformed XccBphP froma bathy-type phytochrome into a canonical one, exhibiting a Pr thermal ground state. The X-ray structures for all the mutants were obtained in the Pr conformation, identical to the one from the wild-type previously determined, showing no significant differences in the quaternary, tertiary or secondary structures. Finally, wetested the in vivo implications of manipulating the XccBphPphotocycle using xanthan production and stomata aperture as thebiological responses of its signaling output. The null mutant complementation experiments show that locking XccBphP in a Pr-likestate (using D199A) or, converting it into a Pr-stabilized phytochrome (using L193N or L193Q) decreases bacterial exopolysaccharide production in dark condition when compared to null mutant. This is reverted when the complemented strains were grown under red light.
publishDate 2020
dc.date.none.fl_str_mv 2020
dc.type.none.fl_str_mv info:eu-repo/semantics/publishedVersion
info:eu-repo/semantics/conferenceObject
Reunión
Book
http://purl.org/coar/resource_type/c_5794
info:ar-repo/semantics/documentoDeConferencia
status_str publishedVersion
format conferenceObject
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/154747
A study on Pr-induced variants of XccBphP bacteriophytochrome photoreceptor from Xanthomonas campestris; V Reunión Grupo Argentino de Fotobiología; La Plata; Argentina; 2020; 1-11
CONICET Digital
CONICET
url http://hdl.handle.net/11336/154747
identifier_str_mv A study on Pr-induced variants of XccBphP bacteriophytochrome photoreceptor from Xanthomonas campestris; V Reunión Grupo Argentino de Fotobiología; La Plata; Argentina; 2020; 1-11
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://grupoargentinodefotobiologia.info/site/site/grupar/pluginfile.php/94/mod_page/content/98/VGRAFOBLibroderesumenes.pdf
info:eu-repo/semantics/altIdentifier/url/https://grupoargentinodefotobiologia.info/site/site/grupar/mod/page/view.php?id=14
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
application/pdf
application/pdf
dc.coverage.none.fl_str_mv Nacional
dc.publisher.none.fl_str_mv Grupo Argentino de Fotobiología
publisher.none.fl_str_mv Grupo Argentino de Fotobiología
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_ 1846083023185903616
score 12.891075

Publicaciones similares