Involvement of the eIF2 alpha Kinase GCN2 in UV-B Responses

GCN2 (general control nonrepressed 2) is a serine/threonine-protein kinase that regulates translation in response to stressors such as amino acid and purin deprivation, cold shock, wounding, cadmium, and UV-C exposure. Activated GCN2 phosphorylates the alpha-subunit of the eukaryotic initiation fact...

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Autores: Llabata, Paula, Richter, Julia, Faus, Isabel, Slominska Durdasiak, Karolina, Hubert Zeh, Lukas, Gadea, Jose, Hauser, Marie Theres
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2019
País:España
Institución:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Repositorio:Recercat. Dipósit de la Recerca de Catalunya
OAI Identifier:oai:recercat.cat:2445/168081
Acceso en línea:https://hdl.handle.net/2445/168081
Access Level:acceso abierto
Palabra clave:Síntesi proteica
Expressió gènica
ADN
Protein synthesis
Gene expression
DNA
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spelling Involvement of the eIF2 alpha Kinase GCN2 in UV-B ResponsesLlabata, PaulaRichter, JuliaFaus, IsabelSlominska Durdasiak, KarolinaHubert Zeh, LukasGadea, JoseHauser, Marie TheresSíntesi proteicaExpressió gènicaADNProtein synthesisGene expressionDNAGCN2 (general control nonrepressed 2) is a serine/threonine-protein kinase that regulates translation in response to stressors such as amino acid and purin deprivation, cold shock, wounding, cadmium, and UV-C exposure. Activated GCN2 phosphorylates the alpha-subunit of the eukaryotic initiation factor 2 (eIF2) leading to a drastic inhibition of protein synthesis and shifting translation to specific mRNAs. To investigate the role of GCN2 in responses to UV-B radiation its activity was analyzed through eIF2 alpha phosphorylation assays in mutants of the specific UV-B and stress signaling pathways of Arabidopsis thaliana. EIF2 alpha phosphorylation was detectable 30 min after UV-B exposure, independent of the UV-B photoreceptor UV RESISTANCE LOCUS8 and its downstream signaling components. GCN2 dependent phosphorylation of eIF2 alpha was also detectable in mutants of the stress related MAP kinases, MPK3 and MPK6 and their negative regulator map kinase phosphatase1 (MKP1). Transcription of downstream components of the UV-B signaling pathway, the Chalcone synthase (CHS) was constitutively higher in gcn2-1 compared to wildtype and further increased upon UV-B while GLUTATHIONE PEROXIDASE7 (GPX7) behaved similarly to wildtype. The UVR8 independent FAD-LINKED OXIDOREDUCTASE (FADox) had a lower basal expression in gcn2-1 which was increased upon UV-B. Since high fluence rates of UV-B induce DNA damage the expression of the RAS ASSOCIATED WITH DIABETES PROTEIN51 (RAD51) was quantified before and after UV-B. While the basal expression was similar to wildtype it was significantly less induced upon UV-B in the gcn2-1 mutant. This expression pattern correlates with the finding that gcn2 mutants develop less cyclobutane pyrimidine dimers after UV-B exposure. Quantification of translation with the puromycination assay revealed that gcn2 mutants have an increased rate of translation which was also higher upon UV-B. Growth of gcn2 mutants to chronic UV-B exposure supports GCN2's role as a negative regulator of UV-B responses. The elevated resistance of gcn2 mutants towards repeated UV-B exposure points to a critical role of GCN2 in the regulation of translation upon UV-B.Frontiers Media Sa2020202020192020info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersion15 p.application/pdfhttps://hdl.handle.net/2445/168081Articles publicats en revistes (Institut d'lnvestigació Biomèdica de Bellvitge (IDIBELL))reponame:Recercat. Dipósit de la Recerca de Catalunyainstname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)InglésReproducció del document publicat a: https://doi.org/10.3389/fpls.2019.01492Frontiers In Plant Science, 2019-11-28, Vol. 10 num. 1492https://doi.org/10.3389/fpls.2019.01492cc by (c) Llabata, Paula et al., 2019http://creativecommons.org/licenses/by/3.0/es/info:eu-repo/semantics/openAccessoai:recercat.cat:2445/1680812026-05-29T05:05:01Z
dc.title.none.fl_str_mv Involvement of the eIF2 alpha Kinase GCN2 in UV-B Responses
title Involvement of the eIF2 alpha Kinase GCN2 in UV-B Responses
spellingShingle Involvement of the eIF2 alpha Kinase GCN2 in UV-B Responses
Llabata, Paula
Síntesi proteica
Expressió gènica
ADN
Protein synthesis
Gene expression
DNA
title_short Involvement of the eIF2 alpha Kinase GCN2 in UV-B Responses
title_full Involvement of the eIF2 alpha Kinase GCN2 in UV-B Responses
title_fullStr Involvement of the eIF2 alpha Kinase GCN2 in UV-B Responses
title_full_unstemmed Involvement of the eIF2 alpha Kinase GCN2 in UV-B Responses
title_sort Involvement of the eIF2 alpha Kinase GCN2 in UV-B Responses
dc.creator.none.fl_str_mv Llabata, Paula
Richter, Julia
Faus, Isabel
Slominska Durdasiak, Karolina
Hubert Zeh, Lukas
Gadea, Jose
Hauser, Marie Theres
author Llabata, Paula
author_facet Llabata, Paula
Richter, Julia
Faus, Isabel
Slominska Durdasiak, Karolina
Hubert Zeh, Lukas
Gadea, Jose
Hauser, Marie Theres
author_role author
author2 Richter, Julia
Faus, Isabel
Slominska Durdasiak, Karolina
Hubert Zeh, Lukas
Gadea, Jose
Hauser, Marie Theres
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv Síntesi proteica
Expressió gènica
ADN
Protein synthesis
Gene expression
DNA
topic Síntesi proteica
Expressió gènica
ADN
Protein synthesis
Gene expression
DNA
description GCN2 (general control nonrepressed 2) is a serine/threonine-protein kinase that regulates translation in response to stressors such as amino acid and purin deprivation, cold shock, wounding, cadmium, and UV-C exposure. Activated GCN2 phosphorylates the alpha-subunit of the eukaryotic initiation factor 2 (eIF2) leading to a drastic inhibition of protein synthesis and shifting translation to specific mRNAs. To investigate the role of GCN2 in responses to UV-B radiation its activity was analyzed through eIF2 alpha phosphorylation assays in mutants of the specific UV-B and stress signaling pathways of Arabidopsis thaliana. EIF2 alpha phosphorylation was detectable 30 min after UV-B exposure, independent of the UV-B photoreceptor UV RESISTANCE LOCUS8 and its downstream signaling components. GCN2 dependent phosphorylation of eIF2 alpha was also detectable in mutants of the stress related MAP kinases, MPK3 and MPK6 and their negative regulator map kinase phosphatase1 (MKP1). Transcription of downstream components of the UV-B signaling pathway, the Chalcone synthase (CHS) was constitutively higher in gcn2-1 compared to wildtype and further increased upon UV-B while GLUTATHIONE PEROXIDASE7 (GPX7) behaved similarly to wildtype. The UVR8 independent FAD-LINKED OXIDOREDUCTASE (FADox) had a lower basal expression in gcn2-1 which was increased upon UV-B. Since high fluence rates of UV-B induce DNA damage the expression of the RAS ASSOCIATED WITH DIABETES PROTEIN51 (RAD51) was quantified before and after UV-B. While the basal expression was similar to wildtype it was significantly less induced upon UV-B in the gcn2-1 mutant. This expression pattern correlates with the finding that gcn2 mutants develop less cyclobutane pyrimidine dimers after UV-B exposure. Quantification of translation with the puromycination assay revealed that gcn2 mutants have an increased rate of translation which was also higher upon UV-B. Growth of gcn2 mutants to chronic UV-B exposure supports GCN2's role as a negative regulator of UV-B responses. The elevated resistance of gcn2 mutants towards repeated UV-B exposure points to a critical role of GCN2 in the regulation of translation upon UV-B.
publishDate 2019
dc.date.none.fl_str_mv 2019
2020
2020
2020
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/2445/168081
url https://hdl.handle.net/2445/168081
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Reproducció del document publicat a: https://doi.org/10.3389/fpls.2019.01492
Frontiers In Plant Science, 2019-11-28, Vol. 10 num. 1492
https://doi.org/10.3389/fpls.2019.01492
dc.rights.none.fl_str_mv cc by (c) Llabata, Paula et al., 2019
http://creativecommons.org/licenses/by/3.0/es/
info:eu-repo/semantics/openAccess
rights_invalid_str_mv cc by (c) Llabata, Paula et al., 2019
http://creativecommons.org/licenses/by/3.0/es/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 15 p.
application/pdf
dc.publisher.none.fl_str_mv Frontiers Media Sa
publisher.none.fl_str_mv Frontiers Media Sa
dc.source.none.fl_str_mv Articles publicats en revistes (Institut d'lnvestigació Biomèdica de Bellvitge (IDIBELL))
reponame:Recercat. Dipósit de la Recerca de Catalunya
instname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
instname_str Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
reponame_str Recercat. Dipósit de la Recerca de Catalunya
collection Recercat. Dipósit de la Recerca de Catalunya
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,811543

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