Implication of two glutathione S-transferases in the optimal metabolism of m-toluate by Sphingomonas yanoikuyae B1 |
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Authors: | Bae Mihyun Sul Woo Jun Koh Sung-Cheol Lee Joon H Zylstra Gerben J Kim Young Min Kimr Eungbin |
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Affiliation: | (1) Department of Biology and Institute of Life Science and Biotechnology, Yonsei University, Seoul, 120-749, Korea;(2) Division of Civil and Environmental Engineering, Korea Maritime University, Pusan, 606-791, Korea;(3) Department of Ophthalmology and Institute of Vision Research, Yonsei University College of Medicine, Seoul, 120-749, Korea;(4) Biotechnology Center for Agriculture and the Environment, Cook College, Rutgers University, New Brunswick, 08901-8520, USA |
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Abstract: | A putative glutathione S-transferase (GST) gene (bphK) was identified in the meta-cleavage operon for the degradation of m-toluate by Sphingomonas yanoikuyae B1. Disruption of bphK resulted in the loss of GST activity against 1-chloro-2,4-dinitrobenzene and a much increased lag time of the mutant strain MB3 (bphK::Km) following subculture into m-toluate medium. In contrast, an increased lag time was not observed when MB3 was grown on biphenyl or m-xylene and MB3 showed normal growth on m-toluate when complemented with a subclone containing the bphK gene only. Furthermore, an additional GST activity was detected in MB3. The induction timing of this second GST activity coincided with the beginning of the exponential growth phase of MB3 on m-toluate, reached maximal activity within three hours, and then dropped sharply to the basal level. Thus, it is apparent that BphK and/or the second GST are necessary for optimal growth of B1 on m-toluate. This revised version was published online in June 2006 with corrections to the Cover Date. |
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Keywords: | Aromatic hydrocarbon Glutathione S-transferase m-toluate Sphingomonas |
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