Catalytic isoforms Tpk1 and Tpk2 of Candida albicans PKA have non-redundant roles in stress response and glycogen storage

Autores
Giacometti, Romina; Kronberg, Maria Florencia; Biondi, Ricardo Miguel; Di Bernardo, Maria Susana
Año de publicación
2009
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Candida albicans cAMP-dependent protein kinase (PKA) is coded by two catalytic subunits (TPK1 and TPK2) and one regulatory subunit (BCY1). In this organism the cAMP/PKA signalling pathway mediates basic cellular processes, such as the yeast-to-hyphae transition and cell cycle regulation. In the present study, we investigated the role of C. albicans PKA in response to saline, heat and oxidative stresses as well as in glycogen storage. To fine-tune the analysis, we performed the studies on several C. albicans PKA mutants having heterozygous or homozygous deletions of TPK1 and/or TPK2 in a different BCY1 genetic background.We observed that tpk1 Δ/tpk1 Δ strains developed a lower tolerance to saline exposure, heat shock and oxidative stress, while wild-type and tpk2 Δ/tpk2 Δ mutants were resistant to these stresses, indicating that both isoforms play different roles in the stress response pathway. We also found that regardless of the TPK background, heterozygous and homozygous BCY1 mutants were highly sensitive to heat treatment. Surprisingly, we observed that those strains devoid of one or both TPK1 alleles were defective in glycogen storage, while strains lacking Tpk2 accumulated higher levels of the polysaccharide, indicating that Tpk1 and Tpk2 have opposite roles in carbohydrate metabolism. Copyright © 2009 John Wiley & Sons, Ltd.
Fil: Giacometti, Romina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Invetigaciones Bioquímicas y Fisiologicas; Argentina
Fil: Kronberg, Maria Florencia. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Invetigaciones Bioquímicas y Fisiologicas; Argentina
Fil: Biondi, Ricardo Miguel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. University of Saarland; Alemania
Fil: Di Bernardo, Maria Susana. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Invetigaciones Bioquímicas y Fisiologicas; Argentina
Materia
CANDIDA ALBICANS
GLYCOGEN REGULATION
PKA
STRESS RESPONSE
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:11336/60776

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spelling Catalytic isoforms Tpk1 and Tpk2 of Candida albicans PKA have non-redundant roles in stress response and glycogen storageGiacometti, RominaKronberg, Maria FlorenciaBiondi, Ricardo MiguelDi Bernardo, Maria SusanaCANDIDA ALBICANSGLYCOGEN REGULATIONPKASTRESS RESPONSEhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Candida albicans cAMP-dependent protein kinase (PKA) is coded by two catalytic subunits (TPK1 and TPK2) and one regulatory subunit (BCY1). In this organism the cAMP/PKA signalling pathway mediates basic cellular processes, such as the yeast-to-hyphae transition and cell cycle regulation. In the present study, we investigated the role of C. albicans PKA in response to saline, heat and oxidative stresses as well as in glycogen storage. To fine-tune the analysis, we performed the studies on several C. albicans PKA mutants having heterozygous or homozygous deletions of TPK1 and/or TPK2 in a different BCY1 genetic background.We observed that tpk1 Δ/tpk1 Δ strains developed a lower tolerance to saline exposure, heat shock and oxidative stress, while wild-type and tpk2 Δ/tpk2 Δ mutants were resistant to these stresses, indicating that both isoforms play different roles in the stress response pathway. We also found that regardless of the TPK background, heterozygous and homozygous BCY1 mutants were highly sensitive to heat treatment. Surprisingly, we observed that those strains devoid of one or both TPK1 alleles were defective in glycogen storage, while strains lacking Tpk2 accumulated higher levels of the polysaccharide, indicating that Tpk1 and Tpk2 have opposite roles in carbohydrate metabolism. Copyright © 2009 John Wiley & Sons, Ltd.Fil: Giacometti, Romina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Invetigaciones Bioquímicas y Fisiologicas; ArgentinaFil: Kronberg, Maria Florencia. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Invetigaciones Bioquímicas y Fisiologicas; ArgentinaFil: Biondi, Ricardo Miguel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. University of Saarland; AlemaniaFil: Di Bernardo, Maria Susana. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Invetigaciones Bioquímicas y Fisiologicas; ArgentinaJohn Wiley & Sons Ltd2009-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/60776Giacometti, Romina; Kronberg, Maria Florencia; Biondi, Ricardo Miguel; Di Bernardo, Maria Susana; Catalytic isoforms Tpk1 and Tpk2 of Candida albicans PKA have non-redundant roles in stress response and glycogen storage; John Wiley & Sons Ltd; Yeast; 26; 5; 12-2009; 273-2850749-503XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1002/yea.1665info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/abs/10.1002/yea.1665info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:06:26Zoai:ri.conicet.gov.ar:11336/60776instacron: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:34982025-09-03 10:06:27.157CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Catalytic isoforms Tpk1 and Tpk2 of Candida albicans PKA have non-redundant roles in stress response and glycogen storage
title Catalytic isoforms Tpk1 and Tpk2 of Candida albicans PKA have non-redundant roles in stress response and glycogen storage
spellingShingle Catalytic isoforms Tpk1 and Tpk2 of Candida albicans PKA have non-redundant roles in stress response and glycogen storage
Giacometti, Romina
CANDIDA ALBICANS
GLYCOGEN REGULATION
PKA
STRESS RESPONSE
title_short Catalytic isoforms Tpk1 and Tpk2 of Candida albicans PKA have non-redundant roles in stress response and glycogen storage
title_full Catalytic isoforms Tpk1 and Tpk2 of Candida albicans PKA have non-redundant roles in stress response and glycogen storage
title_fullStr Catalytic isoforms Tpk1 and Tpk2 of Candida albicans PKA have non-redundant roles in stress response and glycogen storage
title_full_unstemmed Catalytic isoforms Tpk1 and Tpk2 of Candida albicans PKA have non-redundant roles in stress response and glycogen storage
title_sort Catalytic isoforms Tpk1 and Tpk2 of Candida albicans PKA have non-redundant roles in stress response and glycogen storage
dc.creator.none.fl_str_mv Giacometti, Romina
Kronberg, Maria Florencia
Biondi, Ricardo Miguel
Di Bernardo, Maria Susana
author Giacometti, Romina
author_facet Giacometti, Romina
Kronberg, Maria Florencia
Biondi, Ricardo Miguel
Di Bernardo, Maria Susana
author_role author
author2 Kronberg, Maria Florencia
Biondi, Ricardo Miguel
Di Bernardo, Maria Susana
author2_role author
author
author
dc.subject.none.fl_str_mv CANDIDA ALBICANS
GLYCOGEN REGULATION
PKA
STRESS RESPONSE
topic CANDIDA ALBICANS
GLYCOGEN REGULATION
PKA
STRESS RESPONSE
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Candida albicans cAMP-dependent protein kinase (PKA) is coded by two catalytic subunits (TPK1 and TPK2) and one regulatory subunit (BCY1). In this organism the cAMP/PKA signalling pathway mediates basic cellular processes, such as the yeast-to-hyphae transition and cell cycle regulation. In the present study, we investigated the role of C. albicans PKA in response to saline, heat and oxidative stresses as well as in glycogen storage. To fine-tune the analysis, we performed the studies on several C. albicans PKA mutants having heterozygous or homozygous deletions of TPK1 and/or TPK2 in a different BCY1 genetic background.We observed that tpk1 Δ/tpk1 Δ strains developed a lower tolerance to saline exposure, heat shock and oxidative stress, while wild-type and tpk2 Δ/tpk2 Δ mutants were resistant to these stresses, indicating that both isoforms play different roles in the stress response pathway. We also found that regardless of the TPK background, heterozygous and homozygous BCY1 mutants were highly sensitive to heat treatment. Surprisingly, we observed that those strains devoid of one or both TPK1 alleles were defective in glycogen storage, while strains lacking Tpk2 accumulated higher levels of the polysaccharide, indicating that Tpk1 and Tpk2 have opposite roles in carbohydrate metabolism. Copyright © 2009 John Wiley & Sons, Ltd.
Fil: Giacometti, Romina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Invetigaciones Bioquímicas y Fisiologicas; Argentina
Fil: Kronberg, Maria Florencia. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Invetigaciones Bioquímicas y Fisiologicas; Argentina
Fil: Biondi, Ricardo Miguel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. University of Saarland; Alemania
Fil: Di Bernardo, Maria Susana. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Invetigaciones Bioquímicas y Fisiologicas; Argentina
description Candida albicans cAMP-dependent protein kinase (PKA) is coded by two catalytic subunits (TPK1 and TPK2) and one regulatory subunit (BCY1). In this organism the cAMP/PKA signalling pathway mediates basic cellular processes, such as the yeast-to-hyphae transition and cell cycle regulation. In the present study, we investigated the role of C. albicans PKA in response to saline, heat and oxidative stresses as well as in glycogen storage. To fine-tune the analysis, we performed the studies on several C. albicans PKA mutants having heterozygous or homozygous deletions of TPK1 and/or TPK2 in a different BCY1 genetic background.We observed that tpk1 Δ/tpk1 Δ strains developed a lower tolerance to saline exposure, heat shock and oxidative stress, while wild-type and tpk2 Δ/tpk2 Δ mutants were resistant to these stresses, indicating that both isoforms play different roles in the stress response pathway. We also found that regardless of the TPK background, heterozygous and homozygous BCY1 mutants were highly sensitive to heat treatment. Surprisingly, we observed that those strains devoid of one or both TPK1 alleles were defective in glycogen storage, while strains lacking Tpk2 accumulated higher levels of the polysaccharide, indicating that Tpk1 and Tpk2 have opposite roles in carbohydrate metabolism. Copyright © 2009 John Wiley & Sons, Ltd.
publishDate 2009
dc.date.none.fl_str_mv 2009-12
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/11336/60776
Giacometti, Romina; Kronberg, Maria Florencia; Biondi, Ricardo Miguel; Di Bernardo, Maria Susana; Catalytic isoforms Tpk1 and Tpk2 of Candida albicans PKA have non-redundant roles in stress response and glycogen storage; John Wiley & Sons Ltd; Yeast; 26; 5; 12-2009; 273-285
0749-503X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/60776
identifier_str_mv Giacometti, Romina; Kronberg, Maria Florencia; Biondi, Ricardo Miguel; Di Bernardo, Maria Susana; Catalytic isoforms Tpk1 and Tpk2 of Candida albicans PKA have non-redundant roles in stress response and glycogen storage; John Wiley & Sons Ltd; Yeast; 26; 5; 12-2009; 273-285
0749-503X
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1002/yea.1665
info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/abs/10.1002/yea.1665
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
application/pdf
dc.publisher.none.fl_str_mv John Wiley & Sons Ltd
publisher.none.fl_str_mv John Wiley & Sons Ltd
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
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