TY - JOUR
T1 - Specific inhibition of cell wall-bound ATPases by fungal suppressor from mycosphaerella pinodes
AU - Kiba, Akinori
AU - Toyoda, Kazuhiro
AU - Ichinose, Yuki
AU - Yamada, Tetsuji
AU - Shiraishi, Tomonori
N1 - Funding Information:
The authors are indebted to Dr. M. Ikeda, Okayama Prefectural University, Soja; Dr. C. Nakamura, Faculty of Agriculture, Kobe University, Kobe; and Dr. S. Shimomura, National Institute of Agrobiological Resources, Tsukuba, Japan, for their valuable suggestions about the ATPases and receptors in plant cells. This research was supported in part by Grants-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan. Financial support from SanIcyo Co., Ltd., Tokyo, and Nippon Steel Corp., Kawasaki, Japan, were also gratefully acknowledged.
PY - 1995/7
Y1 - 1995/7
N2 - Activities of phosphatases were found in the fractions which were solubilized from cell walls of both pea and cowpea seedlings with 0.5 M NaCl. These phosphatases hydrolyzed triphosphonucleotides in the order: UTP=CTP>GTP>ATP; and UTP=GTP>CTP=ATP, respectively. The activities of a pyrophosphatase and a p-nitrophenylphosphatase were also detected in these fractions. The suppressor in the spore germination fluid of a pea pathogen,Mycosphaerella pinodes, inhibited all of these phosphatase activities in the fraction solubilized from pea cell walls, but it rather enhanced only the activity of the ATPase among those phosphatases from the cowpea cell wall. Hydrolysis of ATP by a cell wall fraction of pea was also markedly inhibited by the suppressor, while hydrolysis of ATP by similar fractions from cowpea, kidney bean and soybean were rather enhanced by the suppressor, as well as by the elicitor. Thus, the cell wall-bound ATPases responded to the suppressor species-specifically. These cell wall-bound ATPases seemed to be different from the plasma membrane ATPases in several respects. The results suggest that plants recognize the fungal signals not only on their plasma membranes but also on their cell walls and, moreover that putative receptors for the fungal signals might be located close to cell wall-bound ATPases or might even be these ATPases themselves.
AB - Activities of phosphatases were found in the fractions which were solubilized from cell walls of both pea and cowpea seedlings with 0.5 M NaCl. These phosphatases hydrolyzed triphosphonucleotides in the order: UTP=CTP>GTP>ATP; and UTP=GTP>CTP=ATP, respectively. The activities of a pyrophosphatase and a p-nitrophenylphosphatase were also detected in these fractions. The suppressor in the spore germination fluid of a pea pathogen,Mycosphaerella pinodes, inhibited all of these phosphatase activities in the fraction solubilized from pea cell walls, but it rather enhanced only the activity of the ATPase among those phosphatases from the cowpea cell wall. Hydrolysis of ATP by a cell wall fraction of pea was also markedly inhibited by the suppressor, while hydrolysis of ATP by similar fractions from cowpea, kidney bean and soybean were rather enhanced by the suppressor, as well as by the elicitor. Thus, the cell wall-bound ATPases responded to the suppressor species-specifically. These cell wall-bound ATPases seemed to be different from the plasma membrane ATPases in several respects. The results suggest that plants recognize the fungal signals not only on their plasma membranes but also on their cell walls and, moreover that putative receptors for the fungal signals might be located close to cell wall-bound ATPases or might even be these ATPases themselves.
KW - Cell wall-bound ATPase
KW - Elicitor
KW - Mycosphaerella pinodes
KW - Pisum sativum L.
KW - Suppressor
KW - Vigna sinensis Endl
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U2 - 10.1093/oxfordjournals.pcp.a078825
DO - 10.1093/oxfordjournals.pcp.a078825
M3 - Article
AN - SCOPUS:0028814110
SN - 0032-0781
VL - 36
SP - 809
EP - 817
JO - Plant and Cell Physiology
JF - Plant and Cell Physiology
IS - 5
ER -