BMB Reports

생화학분자생물학회 (Korean Society for Biochemistry and Molecular Biology)
권호 표지
DOI QR코드

DOI QR Code

Chloroplast-type Ferredoxin Involved in Reactivation of Catechol 2,3-Dioxygenase from Pseudomonas sp.S-47

  • Park, Dong-Woo (Department of Microbiology and Biotechnology, and Research Institute for Genetic Engineering, Chungbuk National University) ;
  • Chae, Jong-Chan (Department of Microbiology and Biotechnology, and Research Institute for Genetic Engineering, Chungbuk National University) ;
  • Kim, Young-Soo (Department of Pharmacy, Chungbuk National University) ;
  • Iida, Toshiya (Laboratory of Microbiology, The Institute of Physical and Chemical Research (RIKEN)) ;
  • Kudo, Toshiaki (Laboratory of Microbiology, The Institute of Physical and Chemical Research (RIKEN)) ;
  • Kim, Chi-Kyung (Department of Microbiology and Biotechnology, and Research Institute for Genetic Engineering, Chungbuk National University)
  • 발행 : 2002.07.31
PDF 다운로드
⟨ 이전 논문 다음 논문 ⟩

초록

Pseudomonas sp. S-47 is capable of degrading catechol and 4-chlorocatechol via the meta-cleavage pathway. XyITE products catalyze the dioxygenation of the aromatics. The sylT of the strain S-47 is located just upstream of the xylE gene. XylT of the strain S-47 is located just upstream of the xylE gene. XyIT is typical chloroplast-type ferredoxin, which is characterized by 4 cystein residues that are located at positions 41, 46, 49, and 81. The chloroplast-type ferredoxin of Pseudomonas sp. S-47 exhibited a 98% identity with that of P. putida mt-2(TOL plasmid) in the amino acid sequence, but only about a 40 to 60% identity with the corresponding enzymes from other organisms. We constructed two recombinant plasmids (pRES1 containing xylTE and pRES101 containing xylE without xylT) in order to examine the function of XyIT for the reactivation of the catechol 2,3-dioxygenase (XyIE) that is oxidized with hydrogen peroxide was recovered in the catechol 2,3-dioxygenase (C23O) activity about 4 mimutes after incubation, but the pRES101 showed no recovery. That means that the typical chloroplast-type ferredoxin (XyIT) of Pseudomonas sp. S-47 is involved in the reactivation of the oxidized C23O in the dioxygenolytic cleavage of aromatic compounds.

키워드

참고문헌

  1. Armengaud, J., Gaillard, J. and Timmis, K N. (2000) A second [2Fe-2S] ferredoxin from Sphingomonas sp. Strain RW1 can function as an electron donor for the dioxin dioxygenase. J. Bacterial. 182, 2238-2244. https://doi.org/10.1128/JB.182.8.2238-2244.2000
  2. Bartels, I., Knackrnuss, H. J. and Reineke, W. (1984) Suicide inactivation of catechol 2,3-dioxygenase from Pseudomanas putida mt-2 by 3-halocatechols. Appl. Environ. Microbial. 47, 500-505.
  3. Cerdan, P., Wasserfallen, A., Rekik, M., Tunrnis, K N. and Harayama, S. (1994) Substrate specificity of catechol 2,3- dioxygenase encoded by TOL plasmid pWW0 of Pseudomonas putida and its relationship to cell growth. J. Bacterial. 176, 6074-6081. https://doi.org/10.1128/jb.176.19.6074-6081.1994
  4. Fujii, T., Takeo, M. and Maeda, Y. (1997) Plasmid-encoded genes specifying aniline oxidation from Acinetobacter sp. strain YAA. Microbiology 143, 93-99. https://doi.org/10.1099/00221287-143-1-93
  5. Furukawa, K, Hirose, J., Suyama, A., Zaiki, T. and Hayashida, S. (1993) Gene components responsible for discrete substrate specificity in the metabolism of biphenyl (bph operon) and toluene (tod operon). J. Bacteriol. 175, 5224-5232. https://doi.org/10.1128/jb.175.16.5224-5232.1993
  6. Harayama, S., Polissi, A. and Rekik, M. (1991) Divergent evolution of chloroplast-type ferredoxins. FEBS Left. 285, 85-88. https://doi.org/10.1016/0014-5793(91)80730-Q
  7. Hugo, N., Armengaud, J., Gaillard, J., Timmis, K N. and Jouanneau, Y. (1998) A novel [2Fe-2S] ferredoxin from Pseudomonas putida mt-2 promotes the reductive reactivation of catechol 2,3-dioxygenase. J. Biol. Chem. 273, 9622-9629. https://doi.org/10.1074/jbc.273.16.9622
  8. Hugo, N., Meyer, C., Armengaud, J., Gaillard, J., Timmis, K N. and Jouanneau, Y. (2000) Characterization of three XylT-like [2Fe-2S] ferredoxins associated with catabolism of cresols or naphthalene: evidence for their involvement in catechol dioxygenase reactivation. J. Bacteriol. 182, 5580-5585. https://doi.org/10.1128/JB.182.19.5580-5585.2000
  9. Kirn, S. and Shin, H.-Y. (2000) Reduction of Azobenzene by purified bovine liver quinone reductase. J. Biochem. Mol. Biol. 33, 321-325
  10. Kim, K P., Seo, D. I., Lee, D. H., Kim, Y. and Kirn, C. K (1998) Cloning and expression in E. coli of the genes responsible for degradation of 4-chlorobenzoate and 4-chlorocatechol from Pseudomonas sp. strain S-47. J. Microbiol. 36, 99-105.
  11. Kim, S. I., Kim, S.-J., Leem, S.-H., Oh, K-H., Kim, S. and Park, Y.-M. (2001) Site-directed mutagenesis of two cysteines (155, 202) in catechol 1,2-dioxygenase $I_{1}$ of Acinetobacter lwoffi K24. J. Biochem. Mol. Biol. 34, 172-175.
  12. Kim, S. I., Kweon, S. M., Kirn, S. and Ha, K-S. (1997) Expression and characterization of cat$A_{1}$ (catechol 1,2-dioxygenase $I_{1}$) of Acinetobacter lwoffi K24 in Escherichiacoli. J. Biochem. Mol. Bioi. 30, 342-345.
  13. Kukor, J. J. and Olsen, R. H. (1996) Catechol 2,3-dioxygenases functional in oxygen-limited (hypoxic) environments. Appl. Environ. Microbiol. 62, 1728-1740.
  14. Manson, J. R. and Canunack, R. (1992) The electron-transport proteins of hydroxylating bacterial dioxygenases. Annu. Rev. Microbiol. 46, 277-305. https://doi.org/10.1146/annurev.mi.46.100192.001425
  15. Mars, A. E., Kingma, J., Kaschabek, S. R., Reineke, W. and Janssen, D. B. (1999) Conversion of 3-chlorocatechol by various catechol 2,3-dioxygenases and sequence analysis of the chlorocatechol dioxygenase resion of Pseudomonas putida GJ3l. J. Bacteriol. 181, 1309-1318.
  16. Ng, L. C., Shingler. V., Sze, C. C. and Poh, C. L. (1994) Cloning and sequences of the first eight genes of the chromosomally encoded (methyl) phenol degradation pathway from Pseudomonas putida P35X. Gene 151, 29-36. https://doi.org/10.1016/0378-1119(94)90629-7
  17. Noh, S. J., Kim, Y.. Min, K. H., Karegoudar, T. B. and Kim, C. K (2000) Cloning and nucleotide sequence analysis of xylE gene responsible for meta-cleavage of 4-chlorocatechol from Pseudomonas sp. S-47. Mol. Cells 10, 475-479.
  18. Nozaki, M., Ono, K, Nakazawa, T., Kotani, S. and Hayashi, O. (1968) Metapyrocatechase. $\Pi$. The role of iron and sultbydryl groups. J. Biol. Chem. 243, 2682-2690.
  19. Polissi, A. and Harayama, S. (1993) In vivo reactivation of catechol 2,3-dioxygenase mediated by a chloroplast-type ferredoxin: a bacterial strategy to expand the substrate specificity of aromatic degradative pathways. EMBO J. 12, 3339-3347.
  20. Sala-Trepat, J. M. and Evans, C. W. (1971) The meta cleavage of catechol by Azotobacter species. 4-Oxalocrotonate pathway. Eur. J. Biochem. 20, 400-413. https://doi.org/10.1111/j.1432-1033.1971.tb01406.x
  21. Sambrook, J., Fritsch, E. F. and Maniatis, T. (2001) Molecular Cloning: A UIboratory Manual. 3rd. ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
  22. Shingler, V., Powlowski, J. and Marklund, U. (1992) Nucleotide sequence and functional analysis of the complete phenol/3,4- dimethylphenol catabolic pathway of Pseudomonas sp. strain CF600. J. Bacterial. 174, 711-724. https://doi.org/10.1128/jb.174.3.711-724.1992
  23. Wasserfallen, A. (1989) Biochemical and genetical study of the specificity of catechol 2,3-dioxygenase from Pseudomonas putida. Ph.D. thesis, University of Geneva.

피인용 문헌

  1. The thermophilic archaeon Sulfolobus solfataricus is able to grow on phenol vol.156, pp.5-6, 2005, https://doi.org/10.1016/j.resmic.2005.04.001
  2. Complete Sequence Determination Combined with Analysis of Transposition/Site-specific Recombination Events to Explain Genetic Organization of IncP-7 TOL Plasmid pWW53 and Related Mobile Genetic Elements vol.369, pp.1, 2007, https://doi.org/10.1016/j.jmb.2007.02.098
  3. Cellular Assays for Ferredoxins: A Strategy for Understanding Electron Flow through Protein Carriers That Link Metabolic Pathways vol.55, pp.51, 2016, https://doi.org/10.1021/acs.biochem.6b00831
  4. Less is more: reduced catechol production permits Pseudomonas putida F1 to grow on styrene vol.158, pp.Pt_11, 2012, https://doi.org/10.1099/mic.0.058230-0