Identification of proteins associated with polyhydroxybutyrate granules from Herbaspirillum seropedicae SmR1--old partners, new players

Herbaspirillum seropedicae is a diazotrophic ß-Proteobacterium found associated with important agricultural crops. This bacterium produces polyhydroxybutyrate (PHB), an aliphatic polyester, as a carbon storage and/or source of reducing equivalents. The PHB polymer is stored as intracellular insolubl...

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Bibliographic Details
Published in:PloS one 2013-09, Vol.8 (9), p.e75066-e75066
Main Authors: Tirapelle, Evandro F, Müller-Santos, Marcelo, Tadra-Sfeir, Michelle Z, Kadowaki, Marco A S, Steffens, Maria B R, Monteiro, Rose A, Souza, Emanuel M, Pedrosa, Fabio O, Chubatsu, Leda S
Format: Article
Language:English
Subjects:
Aliphatic compounds
Bacteria
Bacterial Proteins - metabolism
Biodegradation
Carbon
Carbon capture and storage
Carbon sequestration
Carbon storage
Chlamydia
Chlamydia trachomatis
Cloning
DNA-Binding Proteins - metabolism
E coli
Electrophoresis, Polyacrylamide Gel
Enzymes
Escherichia coli
Gene Expression Regulation, Bacterial
Genes
Genes, Bacterial
Genomics
Granular materials
Granules
Herbaspirillum - genetics
Herbaspirillum - metabolism
Hydroxybutyrates - metabolism
Identification
Localization
Mass Spectrometry
Mass spectroscopy
Metabolism
Polyhydroxybutyrate
Polyhydroxybutyric acid
Polymers
Proteins
Proteomics
Synthesis
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Summary:Herbaspirillum seropedicae is a diazotrophic ß-Proteobacterium found associated with important agricultural crops. This bacterium produces polyhydroxybutyrate (PHB), an aliphatic polyester, as a carbon storage and/or source of reducing equivalents. The PHB polymer is stored as intracellular insoluble granules coated mainly with proteins, some of which are directly involved in PHB synthesis, degradation and granule biogenesis. In this work, we have extracted the PHB granules from H. seropedicae and identified their associated-proteins by mass spectrometry. This analysis allowed us to identify the main phasin (PhaP1) coating the PHB granule as well as the PHB synthase (PhbC1) responsible for its synthesis. A phbC1 mutant is impaired in PHB synthesis, confirming its role in H. seropedicae. On the other hand, a phaP1 mutant produces PHB granules but coated mainly with the secondary phasin (PhaP2). Furthermore, some novel proteins not previously described to be involved with PHB metabolism were also identified, bringing new possibilities to PHB function in H. seropedicae.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0075066