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

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It was found that NTPases were bound to cell walls of pea and cowpea. The suppressor in pycnospore germina-tion 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 con-tained plural molecules that hydrolyze ATP. The M_rs 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 PP_i. The respective electroeluted ATPases also showed the species-specific response to the sup-pressor. 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.
日本植物生理学会の論文