sodium-dodecyl-sulfate and 2-5-dichlorohydroquinone

sodium-dodecyl-sulfate has been researched along with 2-5-dichlorohydroquinone* in 1 studies

Other Studies

1 other study(ies) available for sodium-dodecyl-sulfate and 2-5-dichlorohydroquinone

Article	Year
Cloning and sequencing of a 2,5-dichlorohydroquinone reductive dehalogenase gene whose product is involved in degradation of gamma-hexachlorocyclohexane by Sphingomonas paucimobilis. Journal of bacteriology, 1998, Volume: 180, Issue:6 Sphingomonas (formerly Pseudomonas) paucimobilis UT26 utilizes gamma-hexachlorocyclohexane (gamma-HCH), a halogenated organic insecticide, as a sole carbon and energy source. In a previous study, we showed that gamma-HCH is degraded to 2,5-dichlorohydroquinone (2,5-DCHQ) (Y. Nagata, R. Ohtomo, K. Miyauchi, M. Fukuda, K. Yano, and M. Takagi, J. Bacteriol. 176:3117-3125, 1994). In the present study, we cloned and characterized a gene, designated linD, directly involved in the degradation of 2,5-DCHQ. The linD gene encodes a peptide of 343 amino acids and has a low level of similarity to proteins which belong to the glutathione S-transferase family. When LinD was overproduced in Escherichia coli, a 40-kDa protein was found after sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Northern blot analysis revealed that expression of the linD gene was induced by 2,5-DCHQ in S. paucimobilis UT26. Thin-layer chromatography and gas chromatography-mass spectrometry analyses with the LinD-overexpressing E. coli cells revealed that LinD converts 2,5-DCHQ rapidly to chlorohydroquinone (CHQ) and also converts CHQ slowly to hydroquinone. LinD activity in crude cell extracts was increased 3.7-fold by the addition of glutathione. All three of the Tn5-induced mutants of UT26, which lack 2,5-DCHQ dehalogenase activity, had rearrangements or a deletion in the linD region. These results indicate that LinD is a glutathione-dependent reductive dehalogenase involved in the degradation of gamma-HCH by S. paucimobilis UT26. Topics: Amino Acid Sequence; Bacterial Proteins; Base Composition; Blotting, Northern; Chromatography, Gas; Chromatography, Thin Layer; Cloning, Molecular; DNA Transposable Elements; DNA, Bacterial; Escherichia coli; Gene Expression; Gene Library; Glutathione; Glutathione Transferase; Hexachlorocyclohexane; Hydrolases; Hydroquinones; Molecular Sequence Data; Plasmids; Pseudomonas; Restriction Mapping; Sequence Alignment; Sequence Analysis, DNA; Sequence Deletion; Sequence Homology, Amino Acid; Sodium Dodecyl Sulfate	1998

Article

Year

Cloning and sequencing of a 2,5-dichlorohydroquinone reductive dehalogenase gene whose product is involved in degradation of gamma-hexachlorocyclohexane by Sphingomonas paucimobilis.

Journal of bacteriology, 1998, Volume: 180, Issue:6

Sphingomonas (formerly Pseudomonas) paucimobilis UT26 utilizes gamma-hexachlorocyclohexane (gamma-HCH), a halogenated organic insecticide, as a sole carbon and energy source. In a previous study, we showed that gamma-HCH is degraded to 2,5-dichlorohydroquinone (2,5-DCHQ) (Y. Nagata, R. Ohtomo, K. Miyauchi, M. Fukuda, K. Yano, and M. Takagi, J. Bacteriol. 176:3117-3125, 1994). In the present study, we cloned and characterized a gene, designated linD, directly involved in the degradation of 2,5-DCHQ. The linD gene encodes a peptide of 343 amino acids and has a low level of similarity to proteins which belong to the glutathione S-transferase family. When LinD was overproduced in Escherichia coli, a 40-kDa protein was found after sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Northern blot analysis revealed that expression of the linD gene was induced by 2,5-DCHQ in S. paucimobilis UT26. Thin-layer chromatography and gas chromatography-mass spectrometry analyses with the LinD-overexpressing E. coli cells revealed that LinD converts 2,5-DCHQ rapidly to chlorohydroquinone (CHQ) and also converts CHQ slowly to hydroquinone. LinD activity in crude cell extracts was increased 3.7-fold by the addition of glutathione. All three of the Tn5-induced mutants of UT26, which lack 2,5-DCHQ dehalogenase activity, had rearrangements or a deletion in the linD region. These results indicate that LinD is a glutathione-dependent reductive dehalogenase involved in the degradation of gamma-HCH by S. paucimobilis UT26.

Topics: Amino Acid Sequence; Bacterial Proteins; Base Composition; Blotting, Northern; Chromatography, Gas; Chromatography, Thin Layer; Cloning, Molecular; DNA Transposable Elements; DNA, Bacterial; Escherichia coli; Gene Expression; Gene Library; Glutathione; Glutathione Transferase; Hexachlorocyclohexane; Hydrolases; Hydroquinones; Molecular Sequence Data; Plasmids; Pseudomonas; Restriction Mapping; Sequence Alignment; Sequence Analysis, DNA; Sequence Deletion; Sequence Homology, Amino Acid; Sodium Dodecyl Sulfate

1998