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...
Guardado en:
| Autores principales: | , , , , , |
|---|---|
| Formato: | JOUR |
| Materias: | |
| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_19326203_v9_n7_p_Mezzina |
| Aporte de: |
| id |
todo:paper_19326203_v9_n7_p_Mezzina |
|---|---|
| record_format |
dspace |
| spelling |
todo:paper_19326203_v9_n7_p_Mezzina2023-10-03T16:35:44Z A phasin with many faces: Structural insights on PhaP from Azotobacter sp. FA8 Mezzina, M.P. Wetzler, D.E. Catone, M.V. Bucci, H. Di Paola, M. Pettinari, M.J. 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar 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 Mezzina, M.P. Wetzler, D.E. Catone, M.V. Bucci, H. Di Paola, M. Pettinari, M.J. 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. |
| format |
JOUR |
| author |
Mezzina, M.P. Wetzler, D.E. Catone, M.V. Bucci, H. Di Paola, M. Pettinari, M.J. |
| author_facet |
Mezzina, M.P. Wetzler, D.E. Catone, M.V. Bucci, H. Di Paola, M. Pettinari, M.J. |
| author_sort |
Mezzina, M.P. |
| 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 |
| url |
http://hdl.handle.net/20.500.12110/paper_19326203_v9_n7_p_Mezzina |
| work_keys_str_mv |
AT mezzinamp aphasinwithmanyfacesstructuralinsightsonphapfromazotobacterspfa8 AT wetzlerde aphasinwithmanyfacesstructuralinsightsonphapfromazotobacterspfa8 AT catonemv aphasinwithmanyfacesstructuralinsightsonphapfromazotobacterspfa8 AT buccih aphasinwithmanyfacesstructuralinsightsonphapfromazotobacterspfa8 AT dipaolam aphasinwithmanyfacesstructuralinsightsonphapfromazotobacterspfa8 AT pettinarimj aphasinwithmanyfacesstructuralinsightsonphapfromazotobacterspfa8 AT mezzinamp phasinwithmanyfacesstructuralinsightsonphapfromazotobacterspfa8 AT wetzlerde phasinwithmanyfacesstructuralinsightsonphapfromazotobacterspfa8 AT catonemv phasinwithmanyfacesstructuralinsightsonphapfromazotobacterspfa8 AT buccih phasinwithmanyfacesstructuralinsightsonphapfromazotobacterspfa8 AT dipaolam phasinwithmanyfacesstructuralinsightsonphapfromazotobacterspfa8 AT pettinarimj phasinwithmanyfacesstructuralinsightsonphapfromazotobacterspfa8 |
| _version_ |
1782024702847352832 |