ArticleJournal of bacteriology2008
Binding of the major phasin, PhaP1, from Ralstonia eutropha H16 to poly(3-hydroxybutyrate) granules.
Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 75 citations in OpenAlex.
- Phasins PhbP2 and PhbP3 Are Involved in the Depolymerization of Polyhydroxybutyrate in Azotobacter vinelandii.Journal of basic microbiology · 2025Article
- N-terminal truncation of PhaCMicrobial cell factories · 2024Article
- The Overexpression of Phasin and Regulator Genes Promoting the Synthesis of Polyhydroxybutyrate in Cupriavidus necator H16 under Nonstress Conditions.Applied and environmental microbiology · 2022Article
- Three-dimensional label-free visualization and quantification of polyhydroxyalkanoates in individual bacterial cell in its native state.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- 3-Hydroxybutyrate as a Metabolite and a Signal Molecule Regulating Processes of Living Organisms.Biomolecules · 2021Review
- In vivo immobilization of an organophosphorus hydrolyzing enzyme on bacterial polyhydroxyalkanoate nano-granules.Microbial cell factories · 2019Article
- Poly(3-Hydroxybutyrate) (PHB) Polymerase PhaC1 and PHB Depolymerase PhaZa1 of Ralstonia eutropha Are PhosphorylatedApplied and environmental microbiology · 2018Article
- Modelling of microbial polyhydroxyalkanoate surface binding protein PhaP for rational mutagenesis.Microbial biotechnology · 2017Article
- Polyhydroxyalkanoate-associated phasins as phylogenetically heterogeneous, multipurpose proteins.Microbial biotechnology · 2017Review
- Genome features of moderately halophilic polyhydroxyalkanoate-producingStandards in genomic sciences · 2017Article
- 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
- Polyhydroxyalkanoate (PHA) Granules Have no Phospholipids.Scientific reports · 2016Article
- Backup Expression of the PhaP2 Phasin Compensates for phaP1 Deletion in Herbaspirillum seropedicae, Maintaining Fitness and PHB Accumulation.Frontiers in microbiology · 2016Article
- Photoautotrophic Polyhydroxybutyrate Granule Formation Is Regulated by Cyanobacterial Phasin PhaP in Synechocystis sp. Strain PCC 6803.Applied and environmental microbiology · 2015Article
- Smart polyhydroxyalkanoate nanobeads by protein based functionalization.Nanomedicine : nanotechnology, biology, and medicine · 2015Review
- Comparative proteome analysis reveals four novel polyhydroxybutyrate (PHB) granule-associated proteins in Ralstonia eutropha H16.Applied and environmental microbiology · 2015Article
- Phasin proteins activate Aeromonas caviae polyhydroxyalkanoate (PHA) synthase but not Ralstonia eutropha PHA synthase.Applied and environmental microbiology · 2014Article
- Accumulation of high-value lipids in single-cell microorganisms: a mechanistic approach and future perspectives.Journal of agricultural and food chemistry · 2014Review
- Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The surface of polyhydroxybutyrate (PHB) storage granules in bacteria is covered mainly by proteins referred to as phasins. The layer of phasins stabilizes the granules and prevents coalescence of separated granules in the cytoplasm and nonspecific binding of other proteins to the hydrophobic surfaces of the granules. Phasin PhaP1(Reu) is the major surface protein of PHB granules in Ralstonia eutropha H16 and occurs along with three homologues (PhaP2, PhaP3, and PhaP4) that have the capacity to bind to PHB granules but are present at minor levels. All four phasins lack a highly conserved domain but share homologous hydrophobic regions. To identify the region of PhaP1(Reu) which is responsible for the binding of the protein to the granules, N-terminal and C-terminal fusions of enhanced green fluorescent protein with PhaP1(Reu) or various regions of PhaP1(Reu) were generated by recombinant techniques. The fusions were localized in the cells of various recombinant strains by fluorescence microscopy, and their presence in different subcellular protein fractions was determined by immunodetection of blotted proteins. The fusions were also analyzed to determine their capacities to bind to isolated PHB granules in vitro. The results of these studies indicated that unlike the phasin of Rhodococcus ruber, there is no discrete binding motif; instead, several regions of PhaP1(Reu) contribute to the binding of this protein to the surface of the granules. The conclusions are supported by the results of a small-angle X-ray scattering analysis of purified PhaP1(Reu), which revealed that PhaP1(Reu) is a planar, triangular protein that occurs as trimer. This study provides new insights into the structure of the PHB granule surface, and the results should also have an impact on potential biotechnological applications of phasin fusion proteins and PHB granules in nanobiotechnology.
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