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Plant Physiol, October 1999, Vol. 121, pp. 391-398
The Enzymatic Activity of Fungal Xylanase Is Not Necessary for
Its Elicitor Activity
Jürg
Enkerli,*
Georg
Felix, and
Thomas
Boller
Friedrich Miescher Institute, P.O. Box 2543, CH-4002 Basel,
Switzerland
Fungal xylanases from
Trichoderma spp. are potent elicitors of defense
responses in various plants. To determine whether enzymatic activity is
necessary for elicitor activity, we used site-directed mutagenesis to
reduce the catalytic activity of xylanase II from Trichoderma
reesei. For this, the glutamic acid residue at position 210, which is part of the active center in this family of enzymes, was
changed to either aspartic acid (E210D) or serine (E210S). Wild-type
and mutated forms of xylanase II were expressed in yeast cells and
purified to homogeneity. Compared with the wild-type form of xylanase
II, E210D had >100-fold and E210S 1,000-fold lower enzymatic activity.
In contrast, these mutated forms showed no comparable drop in elicitor
activity. They fully stimulated medium alkalinization and ethylene
biosynthesis in suspension-cultured tomato (Lycopersicon
esculentum) cells, as well as hypersensitive necrosis in leaves
of tomato and tobacco (Nicotiana tabacum) plants. These
results provide direct evidence that enzyme activity is not necessary
for elicitor activity of fungal xylanase.
*
Corresponding author; e-mail jenkerli{at}fmi.ch; fax
41-61-697-39-76.
© 1999 American Society of Plant Physiologists
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