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Archives of Microbiology

, Volume 178, Issue 5, pp 351–357 | Cite as

The cbs mutant strain of Rhodococcus erythropolis KA2-5-1 expresses high levels of Dsz enzymes in the presence of sulfate

  • Yasuhiro Tanaka
  • Osamu Yoshikawa
  • Kenji Maruhashi
  • Ryuichiro Kurane
Original Paper

Abstract.

Two mutants of the dibenzothiophene-desulfurizing Rhodococcus erythropolis KA2-5-1, strains MS51 and MS316, which express a high level of desulfurizing activity in the presence of sulfate, were isolated using the transposome technique. The level of dibenzothiophene-desulfurization by cell-free extracts prepared from mutants MS51 and MS316 grown on sulfate was about five-fold higher than that by cell-free extracts of the wild-type. This result was consistent with results of Western-blot analysis using antisera specific for DszA, DszB and DszC, the enzymes involved in the desulfurization of dibenzothiophene. Gene analysis of the mutants revealed that the same gene was disrupted in mutants MS51 and MS316 and that the transposon-inserted gene in these strains was the gene for cystathionine β-synthase, cbs. The cbs mutants also expressed high levels of Dsz enzymes when methionine was used as the sole source of sulfur.

Cysteine biosynthesis Desulfurization Rhodococcus erythropolis Transposome Dibenzothiophene 

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Copyright information

© Springer-Verlag 2002

Authors and Affiliations

  • Yasuhiro Tanaka
    • 1
  • Osamu Yoshikawa
    • 1
  • Kenji Maruhashi
    • 1
  • Ryuichiro Kurane
    • 2
  1. 1.Bio-Refining Process Laboratory, Japan Cooperation Center, Petroleum, 1900 Sodeshi, Shimizu, Shizuoka 424-0037, Japan
  2. 2.Research Institute of Biological Resources, National Institute of Advanced Industrial Science and Technology, Central 6, 1-1-1 Higashi, Tsukuba, Ibaraki 305–8566, Japan

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