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Plant and Cell Physiology, 1996, Vol. 37, No. 2 207-214
© 1996

Specific Response of Partially Purified Cell Wall-Bound ATPases to Fungal Suppressor

Akinori Kiba, Kazuhiro Toyoda, Yuki Ichinose, Tetsuji Yamada and Tomonori Shiraishi

Laboratory of Plant Pathology and Genetic Engineering, College of Agriculture, Okayama University Okayama, 700 Japan

It was found that NTPases were bound to cell walls of pea and cowpea. The suppressor in pycnospore germination fluid of a pea pathogen, Mycosphaerella pinodes, inhibited the ATPase activity in the fraction, which was solubilized from pea cell wall with 0.5% Triton X-100, in a dose-dependent manner, but rather enhanced that from cowpea cell wall even at the concentration of 1 µg ml-1. Inhibition by the suppressor of pea cell wall-bound ATPase was a mixed type of competitive and noncompetitive. Triton X-100 PAGE and active staining of ATPase indicated that both Triton X-100 solubilized fractions contained plural molecules that hydrolyze ATP. The Mrs of cell wall-bound ATPases seem to be considerably different from those of plasma membranes, and the number of cell wall-bound ATPase molecules were different between pea and cowpea. The electroeluted fractions corresponding to the bands of active-stained ATPases were also able to hydrolyze NTP and PPi. The respective electroeluted ATPases also showed the species-specific response to the suppressor. These results may confirm our previous concept that putative receptors for the suppressor might tightly bind to cell wall-bound ATPase or that the ATPase might be the receptor itself.

(Received September 8, 1995; Accepted March 9, 1996)
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