A phasin with extra talents: A polyhydroxyalkanoate granule associated protein has chaperone activity
- Autores
- Mezzina, Mariela Paula; Wetzler, Diana Elena; de Almeida, Alejandra; Dinjaski, Nina; Prieto, M, A; Pettinari, María Julia
- Año de publicación
- 2015
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Phasins are proteins associated to intracellular polyhydroxyalkanoate granules that affect polymer accumulation and the number and size of the granules. Previous work demonstrated that a phasin from Azotobacter sp FA-8 (PhaPAz) had an unexpected growth-promoting and stress-protecting effect in Escherichia coli, suggesting it could have chaperone-like activities. In this work, in vitro and in vivo experiments were performed in order to investigate this possibility. PhaPAz was shown to prevent in vitro thermal aggregation of the model protein citrate synthase and to facilitate the refolding process of this enzyme after chemical denaturation. Microscopy techniques were used to analyse the subcellular localization of PhaPAz in E.coli strains and to study the role of PhaPAz in in vivo protein folding and aggregation. PhaPAz was shown to colocalize with inclusion bodies of PD, a protein that aggregates when overexpressed. A reduction in the number of inclusion bodies of PD was observed when it was coexpressed with PhaPAz or with the known chaperone GroELS. These results demonstrate that PhaPAz has chaperone-like functions both in vitro and in vivo in E.coli recombinants, and suggests that phasins could have a general protective role in natural polyhydroxyalkanoate producers.
Fil: Mezzina, Mariela Paula. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Wetzler, Diana Elena. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina
Fil: de Almeida, Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Dinjaski, Nina. Consejo Superior de Investigaciones Científicas. Centro de Investigaciones Biológicas; España
Fil: Prieto, M, A. Consejo Superior de Investigaciones Científicas. Centro de Investigaciones Biológicas; España
Fil: Pettinari, María Julia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina - Materia
-
PHASIN
PHAP
AZOTOBACTER
CHAPERONE - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/182491
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A phasin with extra talents: A polyhydroxyalkanoate granule associated protein has chaperone activityMezzina, Mariela PaulaWetzler, Diana Elenade Almeida, AlejandraDinjaski, NinaPrieto, M, APettinari, María JuliaPHASINPHAPAZOTOBACTERCHAPERONEhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Phasins are proteins associated to intracellular polyhydroxyalkanoate granules that affect polymer accumulation and the number and size of the granules. Previous work demonstrated that a phasin from Azotobacter sp FA-8 (PhaPAz) had an unexpected growth-promoting and stress-protecting effect in Escherichia coli, suggesting it could have chaperone-like activities. In this work, in vitro and in vivo experiments were performed in order to investigate this possibility. PhaPAz was shown to prevent in vitro thermal aggregation of the model protein citrate synthase and to facilitate the refolding process of this enzyme after chemical denaturation. Microscopy techniques were used to analyse the subcellular localization of PhaPAz in E.coli strains and to study the role of PhaPAz in in vivo protein folding and aggregation. PhaPAz was shown to colocalize with inclusion bodies of PD, a protein that aggregates when overexpressed. A reduction in the number of inclusion bodies of PD was observed when it was coexpressed with PhaPAz or with the known chaperone GroELS. These results demonstrate that PhaPAz has chaperone-like functions both in vitro and in vivo in E.coli recombinants, and suggests that phasins could have a general protective role in natural polyhydroxyalkanoate producers.Fil: Mezzina, Mariela Paula. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; ArgentinaFil: Wetzler, Diana Elena. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; ArgentinaFil: de Almeida, Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; ArgentinaFil: Dinjaski, Nina. Consejo Superior de Investigaciones Científicas. Centro de Investigaciones Biológicas; EspañaFil: Prieto, M, A. Consejo Superior de Investigaciones Científicas. Centro de Investigaciones Biológicas; EspañaFil: Pettinari, María Julia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; ArgentinaWiley Blackwell Publishing, Inc2015-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/182491Mezzina, Mariela Paula; Wetzler, Diana Elena; de Almeida, Alejandra; Dinjaski, Nina; Prieto, M, A; et al.; A phasin with extra talents: A polyhydroxyalkanoate granule associated protein has chaperone activity; Wiley Blackwell Publishing, Inc; Environmental Microbiology; 17; 5; 5-2015; 1765-17761462-2912CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1111/1462-2920.12636info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:33:54Zoai:ri.conicet.gov.ar:11336/182491instacron: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:34982025-09-29 09:33:55.089CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
A phasin with extra talents: A polyhydroxyalkanoate granule associated protein has chaperone activity |
title |
A phasin with extra talents: A polyhydroxyalkanoate granule associated protein has chaperone activity |
spellingShingle |
A phasin with extra talents: A polyhydroxyalkanoate granule associated protein has chaperone activity Mezzina, Mariela Paula PHASIN PHAP AZOTOBACTER CHAPERONE |
title_short |
A phasin with extra talents: A polyhydroxyalkanoate granule associated protein has chaperone activity |
title_full |
A phasin with extra talents: A polyhydroxyalkanoate granule associated protein has chaperone activity |
title_fullStr |
A phasin with extra talents: A polyhydroxyalkanoate granule associated protein has chaperone activity |
title_full_unstemmed |
A phasin with extra talents: A polyhydroxyalkanoate granule associated protein has chaperone activity |
title_sort |
A phasin with extra talents: A polyhydroxyalkanoate granule associated protein has chaperone activity |
dc.creator.none.fl_str_mv |
Mezzina, Mariela Paula Wetzler, Diana Elena de Almeida, Alejandra Dinjaski, Nina Prieto, M, A Pettinari, María Julia |
author |
Mezzina, Mariela Paula |
author_facet |
Mezzina, Mariela Paula Wetzler, Diana Elena de Almeida, Alejandra Dinjaski, Nina Prieto, M, A Pettinari, María Julia |
author_role |
author |
author2 |
Wetzler, Diana Elena de Almeida, Alejandra Dinjaski, Nina Prieto, M, A Pettinari, María Julia |
author2_role |
author author author author author |
dc.subject.none.fl_str_mv |
PHASIN PHAP AZOTOBACTER CHAPERONE |
topic |
PHASIN PHAP AZOTOBACTER CHAPERONE |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
Phasins are proteins associated to intracellular polyhydroxyalkanoate granules that affect polymer accumulation and the number and size of the granules. Previous work demonstrated that a phasin from Azotobacter sp FA-8 (PhaPAz) had an unexpected growth-promoting and stress-protecting effect in Escherichia coli, suggesting it could have chaperone-like activities. In this work, in vitro and in vivo experiments were performed in order to investigate this possibility. PhaPAz was shown to prevent in vitro thermal aggregation of the model protein citrate synthase and to facilitate the refolding process of this enzyme after chemical denaturation. Microscopy techniques were used to analyse the subcellular localization of PhaPAz in E.coli strains and to study the role of PhaPAz in in vivo protein folding and aggregation. PhaPAz was shown to colocalize with inclusion bodies of PD, a protein that aggregates when overexpressed. A reduction in the number of inclusion bodies of PD was observed when it was coexpressed with PhaPAz or with the known chaperone GroELS. These results demonstrate that PhaPAz has chaperone-like functions both in vitro and in vivo in E.coli recombinants, and suggests that phasins could have a general protective role in natural polyhydroxyalkanoate producers. Fil: Mezzina, Mariela Paula. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina Fil: Wetzler, Diana Elena. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina Fil: de Almeida, Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina Fil: Dinjaski, Nina. Consejo Superior de Investigaciones Científicas. Centro de Investigaciones Biológicas; España Fil: Prieto, M, A. Consejo Superior de Investigaciones Científicas. Centro de Investigaciones Biológicas; España Fil: Pettinari, María Julia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina |
description |
Phasins are proteins associated to intracellular polyhydroxyalkanoate granules that affect polymer accumulation and the number and size of the granules. Previous work demonstrated that a phasin from Azotobacter sp FA-8 (PhaPAz) had an unexpected growth-promoting and stress-protecting effect in Escherichia coli, suggesting it could have chaperone-like activities. In this work, in vitro and in vivo experiments were performed in order to investigate this possibility. PhaPAz was shown to prevent in vitro thermal aggregation of the model protein citrate synthase and to facilitate the refolding process of this enzyme after chemical denaturation. Microscopy techniques were used to analyse the subcellular localization of PhaPAz in E.coli strains and to study the role of PhaPAz in in vivo protein folding and aggregation. PhaPAz was shown to colocalize with inclusion bodies of PD, a protein that aggregates when overexpressed. A reduction in the number of inclusion bodies of PD was observed when it was coexpressed with PhaPAz or with the known chaperone GroELS. These results demonstrate that PhaPAz has chaperone-like functions both in vitro and in vivo in E.coli recombinants, and suggests that phasins could have a general protective role in natural polyhydroxyalkanoate producers. |
publishDate |
2015 |
dc.date.none.fl_str_mv |
2015-05 |
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/11336/182491 Mezzina, Mariela Paula; Wetzler, Diana Elena; de Almeida, Alejandra; Dinjaski, Nina; Prieto, M, A; et al.; A phasin with extra talents: A polyhydroxyalkanoate granule associated protein has chaperone activity; Wiley Blackwell Publishing, Inc; Environmental Microbiology; 17; 5; 5-2015; 1765-1776 1462-2912 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/182491 |
identifier_str_mv |
Mezzina, Mariela Paula; Wetzler, Diana Elena; de Almeida, Alejandra; Dinjaski, Nina; Prieto, M, A; et al.; A phasin with extra talents: A polyhydroxyalkanoate granule associated protein has chaperone activity; Wiley Blackwell Publishing, Inc; Environmental Microbiology; 17; 5; 5-2015; 1765-1776 1462-2912 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/doi/10.1111/1462-2920.12636 |
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.publisher.none.fl_str_mv |
Wiley Blackwell Publishing, Inc |
publisher.none.fl_str_mv |
Wiley Blackwell Publishing, Inc |
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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1844613045997797376 |
score |
13.070432 |