ArticleFEMS microbiology letters2018
Poly(3-hydroxybutyrate) hyperproduction by a global nitrogen regulator NtrB mutant strain of Paracoccus denitrificans PD1222.
Article in FEMS microbiology letters, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 19 citations in OpenAlex.
- Exploring new approaches to enhance polyhydroxybutyrate accumulation in Paracoccus denitrificans.World journal of microbiology & biotechnology · 2026Article
- Identification and Characterization of an R-M System inJournal of microbiology and biotechnology · 2024Article
- Natural Polyhydroxyalkanoates-An Overview of Bacterial Production Methods.Molecules (Basel, Switzerland) · 2024Review
- The NtrYX Two-Component System ofInternational journal of molecular sciences · 2022Article
- Sea-Ice BacteriaApplied and environmental microbiology · 2021Article
- Imaging and modelling of poly(3-hydroxybutyrate) synthesis in Paracoccus denitrificans.AMB Express · 2021Article
- Economic and environmental assessment of bacterial poly(3-hydroxybutyrate) production from the organic fraction of municipal solid waste.Bioresources and bioprocessing · 2021Article
- The Modification of Regulatory Circuits Involved in the Control of Polyhydroxyalkanoates Metabolism to Improve Their Production.Frontiers in bioengineering and biotechnology · 2020Review
- Designing and EngineeringFrontiers in microbiology · 2019Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Paracoccus denitrificans PD1222 accumulates short-length polyhydroxyalkanoates, poly(3-hydroxybutyrate), under nitrogen-deficient conditions. Polyhydroxybutyrate metabolism requires the 3-ketoacyl-CoA thiolase PhaA, the acetoacetyl-CoA dehydrogenase/reductase PhaB and the synthase PhaC for polymerization. Additionally, P. denitrificans PD1222 grows aerobically with nitrate as sole nitrogen source. Nitrate assimilation is controlled negatively by ammonium through the two-component NtrBC system. NtrB is a sensor kinase that autophosphorylates a histidine residue under low-nitrogen concentrations and, in turn, transfers a phosphoryl group to an aspartate residue of the response regulator NtrC protein, which acts as a transcriptional activator of the P. denitrificans PD1222 nasABGHC genes. The P. denitrificans PD1222 NtrB mutant was unable to use nitrate efficiently as nitrogen source when compared to the wild-type strain, and it also overproduced poly(3-hydroxybutyrate). Acetyl-CoA concentration in the P. denitrificans PD1222 NtrB mutant strain was higher than in the wild-type strain. The expression of the phaC gene was also increased in the NtrB mutant when compared to the wild-type strain. These results suggest that accumulation of poly(3-hydroxybutyrate) in the NtrB mutant strain of PD1222 responds to the high levels of acetyl-CoA that accumulate in the cytoplasm as consequence of its inability to efficiently use nitrate as nitrogen source.
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