A phasin with many faces: Structural insights on PhaP from Azotobacter sp. FA8

Phasins are a group of proteins associated to granules of polyhydroxyalkanoates (PHAs). Apart from their structural role as part of the PHA granule cover, different structural and regulatory functions have been found associated to many of them, and several biotechnological applications have been dev...

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Autores principales:	Wetzler, Diana E., Catone, Mariela Verónica
Publicado:	2014
Materias:	bacterial protein PhaP protein phasin polyhydroxyalkanoic acid tetramer unclassified drug DNA binding protein PHAP protein, Bacteria alpha helix amino acid composition amino acid sequence article Azotobacter controlled study hydrophobicity nonhuman protein denaturation protein domain protein quaternary structure protein secondary structure protein unfolding structure analysis chemical phenomena chemistry circular dichroism molecular genetics size exclusion chromatography Bacterial Proteins Chromatography, Gel Circular Dichroism DNA-Binding Proteins Hydrophobic and Hydrophilic Interactions Molecular Sequence Data Protein Structure, Secondary
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_19326203_v9_n7_p_Mezzina http://hdl.handle.net/20.500.12110/paper_19326203_v9_n7_p_Mezzina
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_19326203_v9_n7_p_Mezzina
record_format	dspace
spelling	paper:paper_19326203_v9_n7_p_Mezzina2023-06-08T16:31:24Z A phasin with many faces: Structural insights on PhaP from Azotobacter sp. FA8 Wetzler, Diana E. Catone, Mariela Verónica bacterial protein PhaP protein phasin polyhydroxyalkanoic acid tetramer unclassified drug bacterial protein DNA binding protein PHAP protein, Bacteria alpha helix amino acid composition amino acid sequence article Azotobacter controlled study hydrophobicity nonhuman protein denaturation protein domain protein quaternary structure protein secondary structure protein unfolding structure analysis Azotobacter chemical phenomena chemistry circular dichroism molecular genetics size exclusion chromatography Azotobacter Bacterial Proteins Chromatography, Gel Circular Dichroism DNA-Binding Proteins Hydrophobic and Hydrophilic Interactions Molecular Sequence Data Protein Structure, Secondary Phasins are a group of proteins associated to granules of polyhydroxyalkanoates (PHAs). Apart from their structural role as part of the PHA granule cover, different structural and regulatory functions have been found associated to many of them, and several biotechnological applications have been developed using phasin protein fusions. Despite their remarkable functional diversity, the structure of these proteins has not been analyzed except in very few studies. PhaP from Azotobacter sp. FA8 (PhaPAz) is a representative of the prevailing type in the multifunctional phasin protein family. Previous work performed in our laboratory using this protein have demonstrated that it has some very peculiar characteristics, such as its stress protecting effects in recombinant Escherichia coli, both in the presence and absence of PHA. The aim of the present work was to perform a structural characterization of this protein, to shed light on its properties. Its aminoacid composition revealed that it lacks clear hydrophobic domains, a characteristic that appears to be common to most phasins, despite their lipid granule binding capacity. The secondary structure of this protein, consisting of α-helices and disordered regions, has a remarkable capacity to change according to its environment. Several experimental data support that it is a tetramer, probably due to interactions between coiled-coil regions. These structural features have also been detected in other phasins, and may be related to their functional diversity. © 2014 Mezzina et al. Fil:Wetzler, D.E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Catone, M.V. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2014 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_19326203_v9_n7_p_Mezzina http://hdl.handle.net/20.500.12110/paper_19326203_v9_n7_p_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	bacterial protein PhaP protein phasin polyhydroxyalkanoic acid tetramer unclassified drug bacterial protein DNA binding protein PHAP protein, Bacteria alpha helix amino acid composition amino acid sequence article Azotobacter controlled study hydrophobicity nonhuman protein denaturation protein domain protein quaternary structure protein secondary structure protein unfolding structure analysis Azotobacter chemical phenomena chemistry circular dichroism molecular genetics size exclusion chromatography Azotobacter Bacterial Proteins Chromatography, Gel Circular Dichroism DNA-Binding Proteins Hydrophobic and Hydrophilic Interactions Molecular Sequence Data Protein Structure, Secondary
spellingShingle	bacterial protein PhaP protein phasin polyhydroxyalkanoic acid tetramer unclassified drug bacterial protein DNA binding protein PHAP protein, Bacteria alpha helix amino acid composition amino acid sequence article Azotobacter controlled study hydrophobicity nonhuman protein denaturation protein domain protein quaternary structure protein secondary structure protein unfolding structure analysis Azotobacter chemical phenomena chemistry circular dichroism molecular genetics size exclusion chromatography Azotobacter Bacterial Proteins Chromatography, Gel Circular Dichroism DNA-Binding Proteins Hydrophobic and Hydrophilic Interactions Molecular Sequence Data Protein Structure, Secondary Wetzler, Diana E. Catone, Mariela Verónica A phasin with many faces: Structural insights on PhaP from Azotobacter sp. FA8
topic_facet	bacterial protein PhaP protein phasin polyhydroxyalkanoic acid tetramer unclassified drug bacterial protein DNA binding protein PHAP protein, Bacteria alpha helix amino acid composition amino acid sequence article Azotobacter controlled study hydrophobicity nonhuman protein denaturation protein domain protein quaternary structure protein secondary structure protein unfolding structure analysis Azotobacter chemical phenomena chemistry circular dichroism molecular genetics size exclusion chromatography Azotobacter Bacterial Proteins Chromatography, Gel Circular Dichroism DNA-Binding Proteins Hydrophobic and Hydrophilic Interactions Molecular Sequence Data Protein Structure, Secondary
description	Phasins are a group of proteins associated to granules of polyhydroxyalkanoates (PHAs). Apart from their structural role as part of the PHA granule cover, different structural and regulatory functions have been found associated to many of them, and several biotechnological applications have been developed using phasin protein fusions. Despite their remarkable functional diversity, the structure of these proteins has not been analyzed except in very few studies. PhaP from Azotobacter sp. FA8 (PhaPAz) is a representative of the prevailing type in the multifunctional phasin protein family. Previous work performed in our laboratory using this protein have demonstrated that it has some very peculiar characteristics, such as its stress protecting effects in recombinant Escherichia coli, both in the presence and absence of PHA. The aim of the present work was to perform a structural characterization of this protein, to shed light on its properties. Its aminoacid composition revealed that it lacks clear hydrophobic domains, a characteristic that appears to be common to most phasins, despite their lipid granule binding capacity. The secondary structure of this protein, consisting of α-helices and disordered regions, has a remarkable capacity to change according to its environment. Several experimental data support that it is a tetramer, probably due to interactions between coiled-coil regions. These structural features have also been detected in other phasins, and may be related to their functional diversity. © 2014 Mezzina et al.
author	Wetzler, Diana E. Catone, Mariela Verónica
author_facet	Wetzler, Diana E. Catone, Mariela Verónica
author_sort	Wetzler, Diana E.
title	A phasin with many faces: Structural insights on PhaP from Azotobacter sp. FA8
title_short	A phasin with many faces: Structural insights on PhaP from Azotobacter sp. FA8
title_full	A phasin with many faces: Structural insights on PhaP from Azotobacter sp. FA8
title_fullStr	A phasin with many faces: Structural insights on PhaP from Azotobacter sp. FA8
title_full_unstemmed	A phasin with many faces: Structural insights on PhaP from Azotobacter sp. FA8
title_sort	phasin with many faces: structural insights on phap from azotobacter sp. fa8
publishDate	2014
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_19326203_v9_n7_p_Mezzina http://hdl.handle.net/20.500.12110/paper_19326203_v9_n7_p_Mezzina
work_keys_str_mv	AT wetzlerdianae aphasinwithmanyfacesstructuralinsightsonphapfromazotobacterspfa8 AT catonemarielaveronica aphasinwithmanyfacesstructuralinsightsonphapfromazotobacterspfa8 AT wetzlerdianae phasinwithmanyfacesstructuralinsightsonphapfromazotobacterspfa8 AT catonemarielaveronica phasinwithmanyfacesstructuralinsightsonphapfromazotobacterspfa8
_version_	1768543580579692544

A phasin with many faces: Structural insights on PhaP from Azotobacter sp. FA8

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