dc.creator | Mezzina, Mariela Paula | |
dc.creator | Wetzler, Diana Elena | |
dc.creator | de Almeida, Alejandra | |
dc.creator | Dinjaski, Nina | |
dc.creator | Prieto, M, A | |
dc.creator | Pettinari, María Julia | |
dc.date | 2015-05 | |
dc.date.accessioned | 2023-08-31T00:19:53Z | |
dc.date.available | 2023-08-31T00:19:53Z | |
dc.identifier | http://hdl.handle.net/11336/182491 | |
dc.identifier | 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 | |
dc.identifier | 1462-2912 | |
dc.identifier | CONICET Digital | |
dc.identifier | CONICET | |
dc.identifier.uri | https://repositorioslatinoamericanos.uchile.cl/handle/2250/8543321 | |
dc.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. | |
dc.description | 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 | |
dc.description | 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 | |
dc.description | 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 | |
dc.description | Fil: Dinjaski, Nina. Consejo Superior de Investigaciones Científicas. Centro de Investigaciones Biológicas; España | |
dc.description | Fil: Prieto, M, A. Consejo Superior de Investigaciones Científicas. Centro de Investigaciones Biológicas; España | |
dc.description | 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 | |
dc.format | application/pdf | |
dc.format | application/pdf | |
dc.format | application/pdf | |
dc.format | application/pdf | |
dc.language | eng | |
dc.publisher | Wiley Blackwell Publishing, Inc | |
dc.relation | info:eu-repo/semantics/altIdentifier/doi/10.1111/1462-2920.12636 | |
dc.rights | info:eu-repo/semantics/openAccess | |
dc.rights | https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ | |
dc.subject | PHASIN | |
dc.subject | PHAP | |
dc.subject | AZOTOBACTER | |
dc.subject | CHAPERONE | |
dc.subject | https://purl.org/becyt/ford/1.6 | |
dc.subject | https://purl.org/becyt/ford/1 | |
dc.title | A phasin with extra talents: A polyhydroxyalkanoate granule associated protein has chaperone activity | |
dc.type | info:eu-repo/semantics/article | |
dc.type | info:ar-repo/semantics/artículo | |
dc.type | info:eu-repo/semantics/publishedVersion | |