Artículo

Mezzina, M.P.; Wetzler, D.E.; de Almeida, A.; Dinjaski, N.; Prieto, M.A.; Pettinari, M.J. "A phasin with extra talents: A polyhydroxyalkanoate granule-associated protein has chaperone activity" (2015) Environmental Microbiology. 17(5):1765-1776
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Abstract:

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. © 2014 Society for Applied Microbiology and John Wiley & Sons Ltd.

Registro:

Documento: Artículo
Título:A phasin with extra talents: A polyhydroxyalkanoate granule-associated protein has chaperone activity
Autor:Mezzina, M.P.; Wetzler, D.E.; de Almeida, A.; Dinjaski, N.; Prieto, M.A.; Pettinari, M.J.
Filiación:Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, IQUIBICEN-CONICET, Buenos Aires, Argentina
Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas, Madrid, Spain
Palabras clave:Azotobacter; Escherichia coli; bacterial protein; chaperone; phasin; plant lectin; polyhydroxyalkanoic acid; Azotobacter; cell inclusion; chemistry; Escherichia coli; genetics; metabolism; protein folding; Azotobacter; Bacterial Proteins; Escherichia coli; Inclusion Bodies; Molecular Chaperones; Plant Lectins; Polyhydroxyalkanoates; Protein Folding
Año:2015
Volumen:17
Número:5
Página de inicio:1765
Página de fin:1776
DOI: http://dx.doi.org/10.1111/1462-2920.12636
Título revista:Environmental Microbiology
Título revista abreviado:Environ. Microbiol.
ISSN:14622912
CODEN:ENMIF
CAS:Bacterial Proteins; Molecular Chaperones; phasin; Plant Lectins; Polyhydroxyalkanoates
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_14622912_v17_n5_p1765_Mezzina

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Citas:

---------- APA ----------
Mezzina, M.P., Wetzler, D.E., de Almeida, A., Dinjaski, N., Prieto, M.A. & Pettinari, M.J. (2015) . A phasin with extra talents: A polyhydroxyalkanoate granule-associated protein has chaperone activity. Environmental Microbiology, 17(5), 1765-1776.
http://dx.doi.org/10.1111/1462-2920.12636
---------- CHICAGO ----------
Mezzina, M.P., Wetzler, D.E., de Almeida, A., Dinjaski, N., Prieto, M.A., Pettinari, M.J. "A phasin with extra talents: A polyhydroxyalkanoate granule-associated protein has chaperone activity" . Environmental Microbiology 17, no. 5 (2015) : 1765-1776.
http://dx.doi.org/10.1111/1462-2920.12636
---------- MLA ----------
Mezzina, M.P., Wetzler, D.E., de Almeida, A., Dinjaski, N., Prieto, M.A., Pettinari, M.J. "A phasin with extra talents: A polyhydroxyalkanoate granule-associated protein has chaperone activity" . Environmental Microbiology, vol. 17, no. 5, 2015, pp. 1765-1776.
http://dx.doi.org/10.1111/1462-2920.12636
---------- VANCOUVER ----------
Mezzina, M.P., Wetzler, D.E., de Almeida, A., Dinjaski, N., Prieto, M.A., Pettinari, M.J. A phasin with extra talents: A polyhydroxyalkanoate granule-associated protein has chaperone activity. Environ. Microbiol. 2015;17(5):1765-1776.
http://dx.doi.org/10.1111/1462-2920.12636