Exemplar Abstract for Sphingobium chlorophenolicum (Nohynek et al. 1996) Takeuchi et al. 2001 emend. Hördt et al. 2020 and Sphingomonas chlorophenolica Nohynek et al. 1996.

2003 ◽  
Author(s):  
Charles Thomas Parker ◽  
Dorothea Taylor ◽  
George M Garrity
2002 ◽  
Vol 184 (17) ◽  
pp. 4672-4680 ◽  
Author(s):  
Mian Cai ◽  
Luying Xun

ABSTRACT The first three enzymes of the pentachlorophenol (PCP) degradation pathway in Sphingobium chlorophenolicum (formerly Sphingomonas chlorophenolica) ATCC 39723 have been characterized, and the corresponding genes, pcpA, pcpB, and pcpC, have been individually cloned and sequenced. To search for new genes involved in PCP degradation and map the physical locations of the pcp genes, a 24-kb fragment containing pcpA and pcpC was completely sequenced. A putative LysR-type transcriptional regulator gene, pcpM, and a maleylacetate reductase gene, pcpE, were identified upstream of pcpA. pcpE was found to play a role in PCP degradation. pcpB was not found on the 24-kb fragment. The four gene products PcpB, PcpC, PcpA, and PcpE were responsible for the metabolism of PCP to 3-oxoadipate in ATCC 39723, and inactivational mutation of each gene disrupted the degradation pathway. The organization of the pcp genes is unusual because the four PCP-degrading genes, pcpA, pcpB, pcpC, and pcpE, were found to be located at four discrete locations. Two hypothetical LysR-type regulator genes, pcpM and pcpR, have been identified; pcpM was not required, but pcpR was essential for the induction of pcpB, pcpA, and pcpE. The coinducers of PcpR were PCP and other polychlorinated phenols. The expression of pcpC was constitutive. Thus, the organization and regulation of the genes involved in PCP degradation to 3-oxoadipate were documented.


1998 ◽  
Vol 44 (7) ◽  
pp. 667-675 ◽  
Author(s):  
Vandana M Saboo ◽  
Michael A Gealt

Bacteria isolated from a pentachlorophenol (PCP) contaminated site grew in the presence of 50 µg PCP/mL but were not able to degrade it in either liquid medium or the presence of 1% sterile potting soil as a solid support. Probes developed using the gene sequence of PCP-4-monooxygenase (pcpB) from Sphingomonas chlorophenolica sp.nov hybridized to two separate isolates. Identification based on fatty acid methyl ester profiles (Sherlock™), substrate utilization (BIOLOG™), and 16S rRNA showed that the two strains were different from each other and from Sphingomonas chlorophenolica. Sequences from these isolates, amplified by polymerase chain reaction, confirmed the homology with pcpB. The presence of pcpB sequences in these nondegraders indicated that growth and hybridization data alone were insufficient for predicting degradation capability. Key words: pentachlorophenol, Sphingomonas chlorophenolica, pcpB gene, pentachlorophenol-4-monooxygenase.


2008 ◽  
Vol 190 (23) ◽  
pp. 7595-7600 ◽  
Author(s):  
Yan Huang ◽  
Randy Xun ◽  
Guanjun Chen ◽  
Luying Xun

ABSTRACT Pentachlorophenol (PCP) is a toxic pollutant. Its biodegradation has been extensively studied in Sphingobium chlorophenolicum ATCC 39723. All enzymes required to convert PCP to a common metabolic intermediate before entering the tricarboxylic acid cycle have been characterized. One of the enzymes is tetrachloro-p-hydroquinone (TeCH) reductive dehalogenase (PcpC), which is a glutathione (GSH) S-transferase (GST). PcpC catalyzes the GSH-dependent conversion of TeCH to trichloro-p-hydroquinone (TriCH) and then to dichloro-p-hydroquinone (DiCH) in the PCP degradation pathway. PcpC is susceptible to oxidative damage, and the damaged PcpC produces glutathionyl (GS) conjugates, GS-TriCH and GS-DiCH, which cannot be further metabolized by PcpC. The fate and effect of GS-hydroquinone conjugates were unknown. A putative GST gene (pcpF) is located next to pcpC on the bacterial chromosome. The pcpF gene was cloned, and the recombinant PcpF was purified. The purified PcpF was able to convert GS-TriCH and GS-DiCH conjugates to TriCH and DiCH, respectively. The GS-hydroquinone lyase reactions catalyzed by PcpF are rather unusual for a GST. The disruption of pcpF in S. chlorophenolicum made the mutant lose the GS-hydroquinone lyase activities in the cell extracts. The mutant became more sensitive to PCP toxicity and had a significantly decreased PCP degradation rate, likely due to the accumulation of the GS-hydroquinone conjugates inside the cell. Thus, PcpF played a maintenance role in PCP degradation and converted the GS-hydroquinone conjugates back to the intermediates of the PCP degradation pathway.


2001 ◽  
Vol 289 (1) ◽  
pp. 161-166 ◽  
Author(s):  
Hong Wang ◽  
Marja A. Tiirola ◽  
Jaakko A. Puhakka ◽  
Markku S. Kulomaa

2014 ◽  
Vol 15 (11) ◽  
pp. 20736-20752 ◽  
Author(s):  
Robert Hayes ◽  
Timothy Moural ◽  
Kevin Lewis ◽  
David Onofrei ◽  
Luying Xun ◽  
...  

Chemosphere ◽  
2007 ◽  
Vol 68 (5) ◽  
pp. 864-870 ◽  
Author(s):  
R.I. Dams ◽  
G.I. Paton ◽  
K. Killham

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Lifeng Chen ◽  
Ed S. Krol ◽  
Meena K. Sakharkar ◽  
Haseeb A. Khan ◽  
Abdullah S. Alhomida ◽  
...  

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