ArticlePloS one2014
A phasin with many faces: structural insights on PhaP from Azotobacter sp. FA8.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Phasins PhbP2 and PhbP3 Are Involved in the Depolymerization of Polyhydroxybutyrate in Azotobacter vinelandii.Journal of basic microbiology · 2025Article
- Environmental matrix and moisture influence soil microbial phenotypes in a simplified porous media incubation.mSystems · 2025Article
- Unraveling the effects of polyhydroxyalkanoates accumulation in Pseudomonas extremaustralis growth and survival under different pH conditions.Extremophiles : life under extreme conditions · 2024Article
- The Absence of Phasins PhbP2 and PhbP3 inPolymers · 2024Article
- Article
- Dissecting the Polyhydroxyalkanoate-Binding Domain of the PhaF Phasin: Rational Design of a Minimized Affinity Tag.Applied and environmental microbiology · 2020Article
- Interaction and Regulation of Carbon, Nitrogen, and Phosphorus Metabolisms in Root Nodules of Legumes.Frontiers in plant science · 2018Review
- Polyhydroxyalkanoate-associated phasins as phylogenetically heterogeneous, multipurpose proteins.Microbial biotechnology · 2017Review
- Modelling of microbial polyhydroxyalkanoate surface binding protein PhaP for rational mutagenesis.Microbial biotechnology · 2017Article
- A New Player in the Biorefineries Field: Phasin PhaP Enhances Tolerance to Solvents and Boosts Ethanol and 1,3-Propanediol Synthesis in Escherichia coli.Applied and environmental microbiology · 2017Article
- Structural Insights on PHA Binding Protein PhaP from Aeromonas hydrophila.Scientific reports · 2016Article
- Phasins, Multifaceted Polyhydroxyalkanoate Granule-Associated Proteins.Applied and environmental microbiology · 2016Review
- Regulation of Polyhydroxybutyrate Synthesis in the Soil Bacterium Bradyrhizobium diazoefficiens.Applied and environmental microbiology · 2016Article
- Article
- Polyhydroxyalkanoate (PHA) Granules Have no Phospholipids.Scientific reports · 2016Article
- Photoautotrophic Polyhydroxybutyrate Granule Formation Is Regulated by Cyanobacterial Phasin PhaP in Synechocystis sp. Strain PCC 6803.Applied and environmental microbiology · 2015Article
- Comparative proteome analysis reveals four novel polyhydroxybutyrate (PHB) granule-associated proteins in Ralstonia eutropha H16.Applied and environmental microbiology · 2015Article
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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