Floral Nectary-specific Gene NTR1 Encodes a Jasmonic Acid Carboxyl Methyltransferase

  • Seo, Hak Soo (School of Agricultural Biotechnology, Seoul National University) ;
  • Song, Jong Tae (School of Agricultural Biotechnology, Seoul National University) ;
  • Koo, Yeon Jong (School of Agricultural Biotechnology, Seoul National University) ;
  • Jung, Choonkyun (School of Agricultural Biotechnology, Seoul National University) ;
  • Yeu, Song Yion (School of Agricultural Biotechnology, Seoul National University) ;
  • Kim, Minkyun (School of Agricultural Biotechnology, Seoul National University) ;
  • Song, Sang Ik (Department of Biological Science, Myongji University) ;
  • Lee, Jong Seob (School of Biological Sciences, Seoul National University) ;
  • Hwang, Ingyu (School of Agricultural Biotechnology, Seoul National University) ;
  • Cheong, Jong-Joo (School of Agricultural Biotechnology, Seoul National University) ;
  • Choi, Yang Do (School of Agricultural Biotechnology, Seoul National University)
  • Received : 2001.09.04
  • Published : 2001.09.30

Abstract

NTR1 gene of Brassica campestris L. ssp. perkinensis encodes a floral nectary-specific methyltransferase. In this study, the NTR1 cDNA was expressed in E. coli to examine the enzymatic characteristics of the protein product. The GST-NTR1 fusion protein was purified to near homogeneity, showing that the size of NTR1 was 44 kDa. The protein reacted specifically with jasmonic acid (JA), consuming methyl group from S-adenosyl-L-methionine (SAM). GC-MS analysis revealed that the compound produced was authentic methyl jasmonate (MeJA), suggesting that NTR1 is an S-adenosyl-L-methionine: jasmonic acid carboxyl methyltransferase. Km values of NTR1 for JA and SAM were 38.0 and $6.4{\mu}M$, respectively. Optimal activity of the NTR1 was observed at $20^{\circ}C$, pH 7.5, in the presence of 100-150 mM KCl. Thus, kinetic properties, thermal characteristics, optimal pH, and ion-dependency of the NTR1 activity were almost identical to those of Arabidopsis JA methyltransferase JMT, indicating that these two proteins are orthologues of each other.

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