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Genome-wide Analysis of Histone Modifications Distribution using the Chromatin Immunoprecipitation Sequencing Method in Magnaporthe oryzae
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Cation dependent O-methyltransferases from rice.

Yoon Jung Lee1, Bong Gyu Kim, Youhoon Chong

  • 1Department of Bioscience and Biotechnology, Bio/Molecular Informatics Center, Konkuk University, Seoul 143-701, South Korea.

Planta
|October 19, 2007
PubMed
Summary

Rice O-methyltransferase (OMT) genes ROMT-15 and -17 methylate plant compounds like flavones. These enzymes require metal ions for activity, crucial for their function in plant biochemistry.

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Area of Science:

  • Plant Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • O-methyltransferases (OMTs) are crucial enzymes in plant secondary metabolism.
  • Understanding OMT substrate specificity and regulation is key to elucidating metabolic pathways.

Purpose of the Study:

  • To clone and characterize two novel rice OMT genes, ROMT-15 and ROMT-17.
  • To investigate the substrate specificity and catalytic mechanism of ROMT-15 and ROMT-17.
  • To determine the role of metal ions in the enzymatic activity of these OMTs.

Main Methods:

  • Cloning of ROMT-15 and ROMT-17 genes from rice.
  • Expression of OMTs as glutathione S-transferase (GST) fusion proteins in Escherichia coli.
  • Enzymatic assays using various substrates like caffeoyl-CoA, flavones, and flavonols.
  • Site-directed mutagenesis to investigate metal binding sites.

Main Results:

  • ROMT-15 and ROMT-17 successfully expressed and purified as GST fusion proteins.
  • Both enzymes metabolized caffeoyl-CoA, flavones, and flavonols with vicinal hydroxyl groups.
  • Distinct substrate specificities were observed between ROMT-15 and ROMT-17.
  • Methylation occurred at the 3'-hydroxyl group of luteolin and quercetin; 3' and 5' hydroxyl groups of myricetin and tricetin.
  • Enzymes demonstrated cation dependency, with mutations in predicted metal-binding sites abolishing activity.

Conclusions:

  • ROMT-15 and ROMT-17 are novel rice OMTs involved in the methylation of flavonoids and related compounds.
  • The enzymes exhibit specificities that contribute to the diversity of methylated metabolites in rice.
  • Metal ions are essential cofactors for the catalytic activity of ROMT-15 and ROMT-17, highlighting their critical role in enzymatic methylation.