ArticlePloS one2014
Proteomic characterization of plasmid pLA1 for biodegradation of polycyclic aromatic hydrocarbons in the marine bacterium, Novosphingobium pentaromativorans US6-1.
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 10 papers.
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10 citing papers in PubMed, 41 citations in OpenAlex.
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- Elucidation of 4-Hydroxybenzoic Acid Catabolic Pathways inInternational journal of molecular sciences · 2024Article
- Genome analysis for the identification of genes involved in phenanthrene biodegradation pathway inFrontiers in bioengineering and biotechnology · 2023Article
- Biotechnological applications of marine bacteria in bioremediation of environments polluted with hydrocarbons and plastics.Applied microbiology and biotechnology · 2021Review
- Biodegradation and Removal of PAHs byJournal of microbiology and biotechnology · 2021Article
- Transcriptome Analysis ofInternational journal of molecular sciences · 2018Article
- Proteomic characterization of the outer membrane vesicle of the halophilic marine bacterium Novosphingobium pentaromativorans US6-1.Journal of microbiology (Seoul, Korea) · 2017Article
- Complete genome sequence of Novosphingobium pentaromativorans US6-1(T).Standards in genomic sciences · 2015Article
- Biodegradation of polycyclic aromatic hydrocarbons by Novosphingobium pentaromativorans US6-1.PloS one · 2014Article
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11 authors at 4 institutions in 1 country.
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Abstract
Novosphingobium pentaromativorans US6-1 is a halophilic marine bacterium able to degrade polycyclic aromatic hydrocarbons (PAHs). Genome sequence analysis revealed that the large plasmid pLA1 present in N. pentaromativorans US6-1 consists of 199 ORFs and possess putative biodegradation genes that may be involved in PAH degradation. 1-DE/LC-MS/MS analysis of N. pentaromativorans US6-1 cultured in the presence of different PAHs and monocyclic aromatic hydrocarbons (MAHs) identified approximately 1,000 and 1,400 proteins, respectively. Up-regulated biodegradation enzymes, including those belonging to pLA1, were quantitatively compared. Among the PAHs, phenanthrene induced the strongest up-regulation of extradiol cleavage pathway enzymes such as ring-hydroxylating dioxygenase, putative biphenyl-2,3-diol 1,2-dioxygenase, and catechol 2,3-dioxygenase in pLA1. These enzymes lead the initial step of the lower catabolic pathway of aromatic hydrocarbons through the extradiol cleavage pathway and participate in the attack of PAH ring cleavage, respectively. However, N. pentaromativorans US6-1 cultured with p-hydroxybenzoate induced activation of another extradiol cleavage pathway, the protocatechuate 4,5-dioxygenase pathway, that originated from chromosomal genes. These results suggest that N. pentaromativorans US6-1 utilizes two different extradiol pathways and plasmid pLA1 might play a key role in the biodegradation of PAH in N. pentaromativorans US6-1.
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