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Title: A SABATH Methyltransferase from the moss Physcomitrella patens catalyzes

Abstract

Known SABATH methyltransferases, all of which were identified from seed plants, catalyze methylation of either the carboxyl group of a variety of low molecular weight metabolites or the nitrogen moiety of precursors of caffeine. In this study, the SABATH family from the bryophyte Physcomitrella patens was identified and characterized. Four SABATH-like sequences (PpSABATH1, PpSABATH2, PpSABATH3, and PpSABATH4) were identified from the P. patens genome. Only PpSABATH1 and PpSABATH2 showed expression in the leafy gametophyte of P. patens. Full-length cDNAs of PpSABATH1 and PpSABATH2 were cloned and expressed in soluble form in Escherichia coli. Recombinant PpSABATH1 and PpSABATH2 were tested for methyltransferase activity with a total of 75 compounds. While showing no activity with carboxylic acids or nitrogen-containing compounds, PpSABATH1 displayed methyltransferase activity with a number of thiols. PpSABATH2 did not show activity with any of the compounds tested. Among the thiols analyzed, PpSABATH1 showed the highest level of activity with thiobenzoic acid with an apparent Km value of 95.5 lM, which is comparable to those of known SABATHs. Using thiobenzoic acid as substrate, GC MS analysis indicated that the methylation catalyzed by PpSABATH1 is on the sulfur atom. The mechanism for S-methylation of thiols catalyzed by PpSABATH1 was partially revealedmore » by homology-based structural modeling. The expression of PpSABATH1 was induced by the treatment of thiobenzoic acid. Further transgenic studies showed that tobacco plants overexpressing PpSABATH1 exhibited enhanced tolerance to thiobenzoic acid, suggesting that PpSABATH1 have a role in the detoxification of xenobiotic thiols.« less

Authors:
 [1];  [2];  [3];  [4];  [3];  [5];  [3];  [4];  [6]
  1. ORNL
  2. Universite Joseph Fourier, France
  3. Department of Plant Sciences, University of Tennessee
  4. Institute of Biological Chemistry, Washington State University
  5. Laboratory of Evolutionary Biology, National Institute for Biology, 38 Nishigounaka
  6. University of Tennessee, Knoxville (UTK)
Publication Date:
Research Org.:
Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
Sponsoring Org.:
USDOE Office of Science (SC)
OSTI Identifier:
1056977
DOE Contract Number:  
DE-AC05-00OR22725
Resource Type:
Journal Article
Journal Name:
Phytochemistry
Additional Journal Information:
Journal Volume: 81; Journal ID: ISSN 0031-9422
Country of Publication:
United States
Language:
English
Subject:
Physcomitrella patens Evolution Transgenic tobacco

Citation Formats

Zhao, Nan, Ferrer, Jean-Luc, Moon, Hong S, Kapteyn, Jeremy, Zhuang, Xiaofeng, Hasebe, Mitsuyasu, Stewart, Neal C., Gang, David R., and Chen, Feng. A SABATH Methyltransferase from the moss Physcomitrella patens catalyzes. United States: N. p., 2012. Web. doi:10.1016/j.phytochem.2012.06.011.
Zhao, Nan, Ferrer, Jean-Luc, Moon, Hong S, Kapteyn, Jeremy, Zhuang, Xiaofeng, Hasebe, Mitsuyasu, Stewart, Neal C., Gang, David R., & Chen, Feng. A SABATH Methyltransferase from the moss Physcomitrella patens catalyzes. United States. doi:10.1016/j.phytochem.2012.06.011.
Zhao, Nan, Ferrer, Jean-Luc, Moon, Hong S, Kapteyn, Jeremy, Zhuang, Xiaofeng, Hasebe, Mitsuyasu, Stewart, Neal C., Gang, David R., and Chen, Feng. Sun . "A SABATH Methyltransferase from the moss Physcomitrella patens catalyzes". United States. doi:10.1016/j.phytochem.2012.06.011.
@article{osti_1056977,
title = {A SABATH Methyltransferase from the moss Physcomitrella patens catalyzes},
author = {Zhao, Nan and Ferrer, Jean-Luc and Moon, Hong S and Kapteyn, Jeremy and Zhuang, Xiaofeng and Hasebe, Mitsuyasu and Stewart, Neal C. and Gang, David R. and Chen, Feng},
abstractNote = {Known SABATH methyltransferases, all of which were identified from seed plants, catalyze methylation of either the carboxyl group of a variety of low molecular weight metabolites or the nitrogen moiety of precursors of caffeine. In this study, the SABATH family from the bryophyte Physcomitrella patens was identified and characterized. Four SABATH-like sequences (PpSABATH1, PpSABATH2, PpSABATH3, and PpSABATH4) were identified from the P. patens genome. Only PpSABATH1 and PpSABATH2 showed expression in the leafy gametophyte of P. patens. Full-length cDNAs of PpSABATH1 and PpSABATH2 were cloned and expressed in soluble form in Escherichia coli. Recombinant PpSABATH1 and PpSABATH2 were tested for methyltransferase activity with a total of 75 compounds. While showing no activity with carboxylic acids or nitrogen-containing compounds, PpSABATH1 displayed methyltransferase activity with a number of thiols. PpSABATH2 did not show activity with any of the compounds tested. Among the thiols analyzed, PpSABATH1 showed the highest level of activity with thiobenzoic acid with an apparent Km value of 95.5 lM, which is comparable to those of known SABATHs. Using thiobenzoic acid as substrate, GC MS analysis indicated that the methylation catalyzed by PpSABATH1 is on the sulfur atom. The mechanism for S-methylation of thiols catalyzed by PpSABATH1 was partially revealed by homology-based structural modeling. The expression of PpSABATH1 was induced by the treatment of thiobenzoic acid. Further transgenic studies showed that tobacco plants overexpressing PpSABATH1 exhibited enhanced tolerance to thiobenzoic acid, suggesting that PpSABATH1 have a role in the detoxification of xenobiotic thiols.},
doi = {10.1016/j.phytochem.2012.06.011},
journal = {Phytochemistry},
issn = {0031-9422},
number = ,
volume = 81,
place = {United States},
year = {2012},
month = {1}
}