Two poplar methyl salicylate esterases display comparable biochemical properties but divergent expression patterns

Phytochemistry. 2009 Jan;70(1):32-9. doi: 10.1016/j.phytochem.2008.11.014. Epub 2009 Jan 10.


Two genes encoding proteins of 98% sequence identity that are highly homologous to tobacco methyl salicylate (MeSA) esterase (SABP2) were identified and cloned from poplar. Proteins encoded by these two genes displayed specific esterase activities towards MeSA to produce salicylic acid, and are named PtSABP2-1 and PtSABP2-2, respectively. Recombinant PtSABP2-1 and PtSABP2-2 exhibited apparent Km values of 68.2+/-3.8microM and 24.6+/-1microM with MeSA, respectively. Structural modeling using the three-dimensional structure of tobacco SABP2 as a template indicated that the active sites of PtSABP2-1 and PtSABP2-2 were highly similar to that of tobacco SABP2. Under normal growing conditions, PtSABP2-1 showed the highest level of expression in leaves and PtSABP2-2 was most highly expressed in roots. In leaf tissues of poplar plants under stress conditions, the expression of PtSABP2-1 was significantly down-regulated by two stress factors, whereas the expression of PtSABP2-2 was significantly up-regulated by four stress factors. The plausible mechanisms leading to these two highly homologous MeSA esterase genes involved in divergent biological processes in poplar are discussed.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Esterases / genetics*
  • Esterases / metabolism*
  • Gene Expression Regulation, Plant / physiology*
  • Models, Molecular
  • Molecular Sequence Data
  • Plant Proteins / genetics
  • Plant Proteins / metabolism
  • Populus / enzymology*
  • Substrate Specificity


  • Plant Proteins
  • Esterases