Predominantly cytoplasmic localization in yeast ASR1, a non-receptor transcription factor from plants
- Autores
- Urtasun, Nicolás; Correa Garcia, Susana Raquel; Iusem, Norberto Daniel; Bermudez Moretti, Mariana
- Año de publicación
- 2010
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- The Asr gene family (named after abscisic acid, stress and ripening), currently classified as a novel group of the LEA superfamily, is exclusively present in the genomes of seed plants, except for the Brassicaceae family. It is associated with water-deficit stress and is involved in adaptation to dry climates. Motivated by separate reports depicting ASR proteins as either transcription factors or chaperones, we decided to determine the intracellular localization of ASR proteins. For that purpose, we employed an in vivo eukaryotic expression system, the heterologous model Saccharomyces cerevisiae, including wild type strains as well as mutants in which the variant ASR1 previously proved to be functionally protective against osmotic stress. Our methodology involved immunofluorescence-based confocal microscopy, without artificially altering the native structure of the protein under study. Results show that, in both normal and osmotic stress conditions, recombinant ASR1 turned out to localize mainly to the cytoplasm, irrespective of the genotype used, revealing a scattered distribution in the form of dots or granules. The results are discussed in terms of a plausible dual (cytoplasmic and nuclear) role of ASR proteins.
Fil: Urtasun, Nicolás. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Correa Garcia, Susana Raquel. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Iusem, Norberto Daniel. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Fisiología, Biología Molecular y Celular; Argentina. Consejo Nacional de Investigaciones Cientificas y Tecnicas. Oficina de Coordinacion Administrativa Ciudad Universitaria. Instituto de Fisiologia, Biologia Molecular y Neurocienciasuniversidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Fisiologia, Biologia Molecular y Neurociencias; Argentina
Fil: Bermudez Moretti, Mariana. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina - Materia
-
ASR PROTEINS
WATER STRESS
INTRACELLULAR LOCALIZATION
SACCHAROMYCES CEREVISIAE
CONFOCAL MICROSCOPY - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/14226
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spelling |
Predominantly cytoplasmic localization in yeast ASR1, a non-receptor transcription factor from plantsUrtasun, NicolásCorrea Garcia, Susana RaquelIusem, Norberto DanielBermudez Moretti, MarianaASR PROTEINSWATER STRESSINTRACELLULAR LOCALIZATIONSACCHAROMYCES CEREVISIAECONFOCAL MICROSCOPYhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The Asr gene family (named after abscisic acid, stress and ripening), currently classified as a novel group of the LEA superfamily, is exclusively present in the genomes of seed plants, except for the Brassicaceae family. It is associated with water-deficit stress and is involved in adaptation to dry climates. Motivated by separate reports depicting ASR proteins as either transcription factors or chaperones, we decided to determine the intracellular localization of ASR proteins. For that purpose, we employed an in vivo eukaryotic expression system, the heterologous model Saccharomyces cerevisiae, including wild type strains as well as mutants in which the variant ASR1 previously proved to be functionally protective against osmotic stress. Our methodology involved immunofluorescence-based confocal microscopy, without artificially altering the native structure of the protein under study. Results show that, in both normal and osmotic stress conditions, recombinant ASR1 turned out to localize mainly to the cytoplasm, irrespective of the genotype used, revealing a scattered distribution in the form of dots or granules. The results are discussed in terms of a plausible dual (cytoplasmic and nuclear) role of ASR proteins.Fil: Urtasun, Nicolás. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Correa Garcia, Susana Raquel. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Iusem, Norberto Daniel. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Fisiología, Biología Molecular y Celular; Argentina. Consejo Nacional de Investigaciones Cientificas y Tecnicas. Oficina de Coordinacion Administrativa Ciudad Universitaria. Instituto de Fisiologia, Biologia Molecular y Neurocienciasuniversidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Fisiologia, Biologia Molecular y Neurociencias; ArgentinaFil: Bermudez Moretti, Mariana. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaBentham Science Publishers2010-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/14226Urtasun, Nicolás; Correa Garcia, Susana Raquel; Iusem, Norberto Daniel; Bermudez Moretti, Mariana; Predominantly cytoplasmic localization in yeast ASR1, a non-receptor transcription factor from plants; Bentham Science Publishers; The Open Biochemistry Journal; 4; 5-2010; 68-711874-091Xenginfo:eu-repo/semantics/altIdentifier/url/https://benthamopen.com/ABSTRACT/TOBIOCJ-4-68info:eu-repo/semantics/altIdentifier/doi/10.2174/1874091X01004010068info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2908927/info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-10T13:02:37Zoai:ri.conicet.gov.ar:11336/14226instacron: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:34982025-09-10 13:02:37.956CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Predominantly cytoplasmic localization in yeast ASR1, a non-receptor transcription factor from plants |
title |
Predominantly cytoplasmic localization in yeast ASR1, a non-receptor transcription factor from plants |
spellingShingle |
Predominantly cytoplasmic localization in yeast ASR1, a non-receptor transcription factor from plants Urtasun, Nicolás ASR PROTEINS WATER STRESS INTRACELLULAR LOCALIZATION SACCHAROMYCES CEREVISIAE CONFOCAL MICROSCOPY |
title_short |
Predominantly cytoplasmic localization in yeast ASR1, a non-receptor transcription factor from plants |
title_full |
Predominantly cytoplasmic localization in yeast ASR1, a non-receptor transcription factor from plants |
title_fullStr |
Predominantly cytoplasmic localization in yeast ASR1, a non-receptor transcription factor from plants |
title_full_unstemmed |
Predominantly cytoplasmic localization in yeast ASR1, a non-receptor transcription factor from plants |
title_sort |
Predominantly cytoplasmic localization in yeast ASR1, a non-receptor transcription factor from plants |
dc.creator.none.fl_str_mv |
Urtasun, Nicolás Correa Garcia, Susana Raquel Iusem, Norberto Daniel Bermudez Moretti, Mariana |
author |
Urtasun, Nicolás |
author_facet |
Urtasun, Nicolás Correa Garcia, Susana Raquel Iusem, Norberto Daniel Bermudez Moretti, Mariana |
author_role |
author |
author2 |
Correa Garcia, Susana Raquel Iusem, Norberto Daniel Bermudez Moretti, Mariana |
author2_role |
author author author |
dc.subject.none.fl_str_mv |
ASR PROTEINS WATER STRESS INTRACELLULAR LOCALIZATION SACCHAROMYCES CEREVISIAE CONFOCAL MICROSCOPY |
topic |
ASR PROTEINS WATER STRESS INTRACELLULAR LOCALIZATION SACCHAROMYCES CEREVISIAE CONFOCAL MICROSCOPY |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
The Asr gene family (named after abscisic acid, stress and ripening), currently classified as a novel group of the LEA superfamily, is exclusively present in the genomes of seed plants, except for the Brassicaceae family. It is associated with water-deficit stress and is involved in adaptation to dry climates. Motivated by separate reports depicting ASR proteins as either transcription factors or chaperones, we decided to determine the intracellular localization of ASR proteins. For that purpose, we employed an in vivo eukaryotic expression system, the heterologous model Saccharomyces cerevisiae, including wild type strains as well as mutants in which the variant ASR1 previously proved to be functionally protective against osmotic stress. Our methodology involved immunofluorescence-based confocal microscopy, without artificially altering the native structure of the protein under study. Results show that, in both normal and osmotic stress conditions, recombinant ASR1 turned out to localize mainly to the cytoplasm, irrespective of the genotype used, revealing a scattered distribution in the form of dots or granules. The results are discussed in terms of a plausible dual (cytoplasmic and nuclear) role of ASR proteins. Fil: Urtasun, Nicolás. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Correa Garcia, Susana Raquel. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Iusem, Norberto Daniel. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Fisiología, Biología Molecular y Celular; Argentina. Consejo Nacional de Investigaciones Cientificas y Tecnicas. Oficina de Coordinacion Administrativa Ciudad Universitaria. Instituto de Fisiologia, Biologia Molecular y Neurocienciasuniversidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Fisiologia, Biologia Molecular y Neurociencias; Argentina Fil: Bermudez Moretti, Mariana. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina |
description |
The Asr gene family (named after abscisic acid, stress and ripening), currently classified as a novel group of the LEA superfamily, is exclusively present in the genomes of seed plants, except for the Brassicaceae family. It is associated with water-deficit stress and is involved in adaptation to dry climates. Motivated by separate reports depicting ASR proteins as either transcription factors or chaperones, we decided to determine the intracellular localization of ASR proteins. For that purpose, we employed an in vivo eukaryotic expression system, the heterologous model Saccharomyces cerevisiae, including wild type strains as well as mutants in which the variant ASR1 previously proved to be functionally protective against osmotic stress. Our methodology involved immunofluorescence-based confocal microscopy, without artificially altering the native structure of the protein under study. Results show that, in both normal and osmotic stress conditions, recombinant ASR1 turned out to localize mainly to the cytoplasm, irrespective of the genotype used, revealing a scattered distribution in the form of dots or granules. The results are discussed in terms of a plausible dual (cytoplasmic and nuclear) role of ASR proteins. |
publishDate |
2010 |
dc.date.none.fl_str_mv |
2010-05 |
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/11336/14226 Urtasun, Nicolás; Correa Garcia, Susana Raquel; Iusem, Norberto Daniel; Bermudez Moretti, Mariana; Predominantly cytoplasmic localization in yeast ASR1, a non-receptor transcription factor from plants; Bentham Science Publishers; The Open Biochemistry Journal; 4; 5-2010; 68-71 1874-091X |
url |
http://hdl.handle.net/11336/14226 |
identifier_str_mv |
Urtasun, Nicolás; Correa Garcia, Susana Raquel; Iusem, Norberto Daniel; Bermudez Moretti, Mariana; Predominantly cytoplasmic localization in yeast ASR1, a non-receptor transcription factor from plants; Bentham Science Publishers; The Open Biochemistry Journal; 4; 5-2010; 68-71 1874-091X |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/https://benthamopen.com/ABSTRACT/TOBIOCJ-4-68 info:eu-repo/semantics/altIdentifier/doi/10.2174/1874091X01004010068 info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2908927/ |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Bentham Science Publishers |
publisher.none.fl_str_mv |
Bentham Science Publishers |
dc.source.none.fl_str_mv |
reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
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CONICET Digital (CONICET) |
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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 |
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12.993085 |