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Kim, Seung-Il,Kukor, Jerome J.,Oh, Kye-Heon,Kahng, Hyung-Yeel Elsevier 2006 Enzyme and microbial technology Vol.40 No.1
<P><B>Abstract</B></P><P><I>Pseudomonas rhodesiae</I> strain KK1 was found to be capable of utilizing a broad range of aromatic compounds as well as polycyclic aromatic hydrocarbons in this study. The Rieske-type iron–sulfur center sequences of dioxygenases obtained from KK1 through PCR process using a universal dioxygenase primer set were used to evaluate catabolic potential for aromatic compounds. Comparative analysis of predicted amino acid sequences from 50 randomly selected dioxygenase clones capable of hydroxylating inactivated aromatic nuclei indicated that the clones from strain KK1 could be divided into five groups. Amino acid sequences of each dioxygenase clone were a part of the genes encoding enzyme for initial catabolism of benzoate, carbazole, <I>p</I>-cumate, naphthalene, phenanthrene, biphenyl, or vanillate. Radiorespirometric analysis revealed that strain KK1 was able to mineralize polycyclic aromatic hydrocarbons such as anthracene, naphthalene and phenanthrene, as well as a nitrogen heterocyclic aromatic compound-like carbazole. Also, it has been found through HPLC analysis that benzoate, biphenyl, <I>p</I>-cumate, and vanillate also could be degraded by strain KK1. These results were consistent with data obtained through analyses of dioxygenase clones and substrate conversion assay, providing the evidence that strain KK1 has the capability to degrade a broad range of aromatic substrates including polycyclic aromatic hydrocarbons.</P>
Physiological and Phylogenetic Analysis of Burkholderia sp.HY1 Capable of Aniline Degradation
Kahng, Hyung Yeel,KuKor, Jerome J.,Oh, Kye Heon 한국미생물 · 생명공학회 2000 Journal of microbiology and biotechnology Vol.10 No.5
A new aniline-utilizing microorganism, strain HY1 obtained from an orchard soil, was characterized by using the BIOLOG system, an analysis of the total cellular fatty acids, and a 16S rDNA sequence. Strain HY1 was identified as a Burkholderia species, and was designated Burkholderia sp. HY1. GC and HPLC analyses revealed that Burkholderia sp. HY1 was able to degrade aniline to produce catechol, which was subsequently converted to cis,cis-muconic acid through an ortho-ring fission pathway under aerobic conditions. Strain HY1 exhibited a drastic reduction in the rate of aniline degradation when glucose was added to the aniline media. However, the addition of peptone or nitrate to the aniline media dramatically accelerated the rate of aniline degradation. A fatty acid analysis showed that strain HY1 was able to produce lipids 16:0, 16:0 20H, and 11 methyl 18:1 ω7c approximately 3.7-, 2.2-, and 6-fold more, respectively, when grown on aniline media than when grown on TSA. An analysis of the 16S rDNA sequence revealed that strain HY1 was very closely related to Burkholderia graminis with 95% similarity based on the alignment of a 1,435 bp fragment. A phylogenetic analysis of the 16S rDNA sequence based on a 1,420 bp multi-alignment showed that strain HY1 was placed among three major clonal types of β-Proteobacteria, including Burkholderia graminis, Burkholderia phenazinium, and Burkholderia glathei. The sequence GAT(C or G)G__, which is highly conserved in several locations in the 16S rDNA gene among the major clonal type strains of β-Proteobacteria, was frequently replaced with GAT(C or G)A__ in the 16S rDNA sequence from strain HY1.
Physiological and Phylogenetic Analysis of Burkholderia sp. HY1 Capable of Aniline Degradation
KAHNG, HYUNG-YEEL,KUKOR, JEROME J.,OH, KYE-HEON 濟州大學校 基礎科學硏究所 2001 基礎科學硏究 Vol.14 No.2
A new aniline-utilizing microorganism, strain HY1 obtained from an orchard soil, was characterized by using the BIOLOG system, an analysis of the total cellular fatty acids, and a 16s rDNA sequence. Strain HY1 was identified as a Burkholderiu species, and was designated Burkholderia sp. HY1. GC and HPLC analyses revealed that Burkholderiu sp. HY1 was able to degrade aniline to produce catechol, which was subsequently converted to cis,cis-muconic acid through an orrho-ring fission pathway under aerobic conditions. Strain HY1 exhibited a drastic reduction in the rate of aniline degradation when glucose was added to the aniline media. However, the addition of peptone or nitrate to the aniline media dramatically accelerated the rate of aniline degradation. A fatty acid analysis showed that strain HY1 was able to produce lipids 16:0,16:0 ZOH, and 1 I methyl 18: 1 ω7c approximately 3.7-, 2.2-, and 6-fold more, respectively, when grown on aniline media than when grown on TSA. An analysis of the 16S rDNA sequence revealed that strain HY1 was very closely related to Burkholderia graminis with 95% similarity based on the alignment of a 1,435 bp fragment. A phylogenetic analysis of the 16S rDNA sequence based on a 1,420 bp multi-alignment showed that strain HY1 was placed among three major clonal types of β-Proteobacteria, including Burkholderiu graminis, Burkholderia phenazinium, and Burkholderia glathei. The sequence GAT(C or G)G, which is highly conserved in several locations in the 16S rDNA gene among the major clonal type strains of β-Proteobacteria, was frequently replaced with GAT(C or G)A in the 16S rDNA sequence from strain HYI.
Kahng, Hyung-Yeel,Kukor, Jerome J.,Oh, Kye-Heon 濟州大學校 基礎科學硏究所 2001 基礎科學硏究 Vol.14 No.2
We have characterized a novel microorganism, strain HY99, which is capable of aerobic and anaerobic degradation of aniline. Strain HY99 was found to aerobically metabolize aniline via catechol and 2-hydroxymuconicsemialdehyde intermediates, and to transform aniline .via p-aminobenzoate in anaerobic environments. Physiological and biochemical tests revealed that strain HY99 was most similar to Delftia acidovorans, but unlike D. acidovorans, strain HY99 was able to metabolize aniline under anaerobic conditions linked with nitrate reduction. Phylogenetic analysis based on 16S rDNA sequencing also revealed that strain HY99 was closely related to D. acidovorans, with 96% overall similarity.
Characterization and Role of tbuX in Utilization of Toluene by Ralstonia pickettii PKO1
KAHNG, HYUNG-YEEL,BYRNE, ARMANDO M.,OLSEN, RONALD H.,KUKOR, JEROME J. 濟州大學校 基礎科學硏究所 2001 基礎科學硏究 Vol.14 No.1
The tbu regulon of Ralstonia pickettii PKOl encodes enzymes involved in the catabolism of toluene, benzene, and related alkylaromatic hydrocarbons. The first operon in this regulon contains genes that encode the tbu pathway's initial catabolic enzyme, toluene-3-monooxygenase, as well as TbuT, the NtrC-like transcriptional activator for the entire regulon. It has been previously shown that the organization of tbuT, which is located immediately downstream of tbuA1UBVA2C, and the associated promoter (PtbuA1) is unique in that it results in a cascade type of up-regulation of tbuT in response to a variety of effector compounds. In our efforts to further characterize this unusual mode of gene regulation, we discovered another open reading frame, encoded on the strand opposite that of tbuT, 63 bp downstream of the tbuT stop codon. The 1,374-bp open reading frame, encoding a 458-amino-acid peptide, was designated tbuX. The predicted amino acid sequence of TbuX exhibited significant similarity to several putative outer membrane proteins from aromatic hydrocarbon-degrading bacteria, as well as to FadL, an outer membrane protein needed for uptake of long-chain fatty acids in Escherichiu coli. Based on sequence analysis, transcriptional and expression studies, and deletion analysis, TbuX seems to play an important role in the catabolism of toluene in R. pickettii PKOl. In addition, the expression of tbuX appears to be regulated in a manner such that low levels of TbuX are always present within the cell, whereas upon toluene exposure these levels dramatically increase, even more than those of toluene- 3-monooxygenase. This expression pattern may relate to the possible role of TbuX as a facilitator of toluene entry into the cell.
KAHNG, HYUNG-YEEL,MALINVERNI, JULIANA C.,MAJKO, MICHELLE M.,KUKOR, JEROME J. 제주대학교 기초과학연구소 2002 基礎科學硏究 Vol.15 No.1
Burkholderia sp. strain JS150 is able to metabolize a wide range of alkyl and chloroaromatic hydrocarbons through multiple, apparently redundant catabolic pahtways. Previous research has shown that strain JS150 is able to synthesize enzymes for multiple upper pathways as well as multiple lower pathways to accommodate variously substituted catechols that result from degradation of complex mixtures of monoaromatic compounds. We report here the genetic organization and functional charcaterization of a gene cluster, designated tbc (for toluene, benzene, and chlorobenzene utilization), which has been cloned as a 14.3 kb DNA fragment from strain JS150 into vector pRO1727. The cloned DNA fragment expressed in Pseudomonas aeruginosa PAOlc allowed the recombinant to grow on toluene or benzene and to transform chlorobenzene, trichloroethylene, phenol, and cresols. The tbc genes are organized into two divergently transcribed operons, tbc1 and tbc2, each comprised of six open reading frames. Similarity searches of databases revealed that the tbc1 and tbc2 genes showed significant homology to multicomponent cresol and phenol hydroxylases and to toluene and benzene monooxygenases, respectively. Deletion mutagenesis and product analysis were used to demonstrate that tbc2 plays a role in the initial catabolism of the unactivated alkyl-or chloroaromatic substrate and that the tbc1 gene products play a role in the catabolism of the first metabolite that results from transformation of the initial substrate. Phylogenetic analysis was used to compare individual components of these tbc monooxygenases with similar sequences in the databases. These results provide further evidence for the existence of multiple, functionally redundant alkyl- and chloroaromatic manaoxygenases in strain JS150.