A phasin with extra talents: A polyhydroxyalkanoate granule-associated protein has chaperone activity

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 (PhaP<inf>Az</inf>) had an unexpected growth-promoting and stress-pro...

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Autor principal: Mezzina, M.P
Otros Autores: Wetzler, D.E, de Almeida, A., Dinjaski, N., Prieto, M.A, Pettinari, M.J
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: Blackwell Publishing Ltd 2015
Acceso en línea:Registro en Scopus
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024 7 |2 scopus  |a 2-s2.0-84928298441 
024 7 |2 cas  |a Bacterial Proteins; Molecular Chaperones; phasin; Plant Lectins; Polyhydroxyalkanoates 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
030 |a ENMIF 
100 1 |a Mezzina, M.P. 
245 1 2 |a A phasin with extra talents: A polyhydroxyalkanoate granule-associated protein has chaperone activity 
260 |b Blackwell Publishing Ltd  |c 2015 
270 1 0 |m Pettinari, M.J.; Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, IQUIBICEN-CONICETArgentina 
506 |2 openaire  |e Política editorial 
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520 3 |a 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 (PhaP<inf>Az</inf>) 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. PhaP<inf>Az</inf> 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 PhaP<inf>Az</inf> in E.coli strains and to study the role of PhaP<inf>Az</inf> in in vivo protein folding and aggregation. PhaP<inf>Az</inf> 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 PhaP<inf>Az</inf> or with the known chaperone GroELS. These results demonstrate that PhaP<inf>Az</inf> 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.  |l eng 
593 |a Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, IQUIBICEN-CONICET, Buenos Aires, Argentina 
593 |a Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas, Madrid, Spain 
690 1 0 |a AZOTOBACTER 
690 1 0 |a ESCHERICHIA COLI 
690 1 0 |a BACTERIAL PROTEIN 
690 1 0 |a CHAPERONE 
690 1 0 |a PHASIN 
690 1 0 |a PLANT LECTIN 
690 1 0 |a POLYHYDROXYALKANOIC ACID 
690 1 0 |a AZOTOBACTER 
690 1 0 |a CELL INCLUSION 
690 1 0 |a CHEMISTRY 
690 1 0 |a ESCHERICHIA COLI 
690 1 0 |a GENETICS 
690 1 0 |a METABOLISM 
690 1 0 |a PROTEIN FOLDING 
690 1 0 |a AZOTOBACTER 
690 1 0 |a BACTERIAL PROTEINS 
690 1 0 |a ESCHERICHIA COLI 
690 1 0 |a INCLUSION BODIES 
690 1 0 |a MOLECULAR CHAPERONES 
690 1 0 |a PLANT LECTINS 
690 1 0 |a POLYHYDROXYALKANOATES 
690 1 0 |a PROTEIN FOLDING 
700 1 |a Wetzler, D.E. 
700 1 |a de Almeida, A. 
700 1 |a Dinjaski, N. 
700 1 |a Prieto, M.A. 
700 1 |a Pettinari, M.J. 
773 0 |d Blackwell Publishing Ltd, 2015  |g v. 17  |h pp. 1765-1776  |k n. 5  |p Environ. Microbiol.  |x 14622912  |w (AR-BaUEN)CENRE-4624  |t Environmental Microbiology 
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