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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Autores principales: Wetzler, Diana E., de Almeida, Alejandra
Publicado: 2015
Materias:
Azotobacter
Escherichia coli
bacterial protein
chaperone
phasin
plant lectin
polyhydroxyalkanoic acid
cell inclusion
chemistry
genetics
metabolism
protein folding
Bacterial Proteins
Inclusion Bodies
Molecular Chaperones
Plant Lectins
Polyhydroxyalkanoates
Protein Folding
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_14622912_v17_n5_p1765_Mezzina
http://hdl.handle.net/20.500.12110/paper_14622912_v17_n5_p1765_Mezzina
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id paper:paper_14622912_v17_n5_p1765_Mezzina
record_format dspace
spelling paper:paper_14622912_v17_n5_p1765_Mezzina2023-06-08T16:16:14Z A phasin with extra talents: A polyhydroxyalkanoate granule-associated protein has chaperone activity Wetzler, Diana E. de Almeida, Alejandra 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 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. Fil:Wetzler, D.E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:de Almeida, A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2015 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_14622912_v17_n5_p1765_Mezzina http://hdl.handle.net/20.500.12110/paper_14622912_v17_n5_p1765_Mezzina
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic 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
spellingShingle 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
Wetzler, Diana E.
de Almeida, Alejandra
A phasin with extra talents: A polyhydroxyalkanoate granule-associated protein has chaperone activity
topic_facet 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
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 (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.
author Wetzler, Diana E.
de Almeida, Alejandra
author_facet Wetzler, Diana E.
de Almeida, Alejandra
author_sort Wetzler, Diana E.
title A phasin with extra talents: A polyhydroxyalkanoate granule-associated protein has chaperone activity
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 phasin with extra talents: a polyhydroxyalkanoate granule-associated protein has chaperone activity
publishDate 2015
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_14622912_v17_n5_p1765_Mezzina
http://hdl.handle.net/20.500.12110/paper_14622912_v17_n5_p1765_Mezzina
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AT dealmeidaalejandra aphasinwithextratalentsapolyhydroxyalkanoategranuleassociatedproteinhaschaperoneactivity
AT wetzlerdianae phasinwithextratalentsapolyhydroxyalkanoategranuleassociatedproteinhaschaperoneactivity
AT dealmeidaalejandra phasinwithextratalentsapolyhydroxyalkanoategranuleassociatedproteinhaschaperoneactivity
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