Specific inhibition of cell wall-bound ATPases by fungal suppressor from mycosphaerella pinodes

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

Research output: Contribution to journalArticle

32 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)809-817
Number of pages9
JournalPlant and Cell Physiology
Volume36
Issue number5
Publication statusPublished - Jul 1995

Fingerprint

Mycosphaerella pinodes
ATP Synthase
Cell Wall
adenosinetriphosphatase
Adenosine Triphosphatases
Cells
cell walls
Adenosinetriphosphate
Phosphatases
Peas
Cowpea
Phosphoric Monoester Hydrolases
phosphatase
peas
Adenosine Triphosphate
cowpeas
Cytidine Triphosphate
Uridine Triphosphate
Plasma Membrane
Cell membranes

Keywords

  • Cell wall-bound ATPase
  • Elicitor
  • Mycosphaerella pinodes
  • Pisum sativum L.
  • Suppressor
  • Vigna sinensis Endl

ASJC Scopus subject areas

  • Statistics, Probability and Uncertainty
  • Applied Mathematics
  • Ecology
  • Cell Biology
  • Physiology
  • Plant Science

Cite this

Specific inhibition of cell wall-bound ATPases by fungal suppressor from mycosphaerella pinodes. / Kiba, Akinori; Toyoda, Kazuhiro; Ichinose, Yuki; Yamada, Tetsuji; Shiraishi, Tomonori.

In: Plant and Cell Physiology, Vol. 36, No. 5, 07.1995, p. 809-817.

Research output: Contribution to journalArticle

@article{43cb93e1b0904ecb94eb105f150017e8,
title = "Specific inhibition of cell wall-bound ATPases by fungal suppressor from mycosphaerella pinodes",
abstract = "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.",
keywords = "Cell wall-bound ATPase, Elicitor, Mycosphaerella pinodes, Pisum sativum L., Suppressor, Vigna sinensis Endl",
author = "Akinori Kiba and Kazuhiro Toyoda and Yuki Ichinose and Tetsuji Yamada and Tomonori Shiraishi",
year = "1995",
month = "7",
language = "English",
volume = "36",
pages = "809--817",
journal = "Plant and Cell Physiology",
issn = "0032-0781",
publisher = "Oxford University Press",
number = "5",

}

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

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

UR - http://www.scopus.com/inward/record.url?scp=0028814110&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028814110&partnerID=8YFLogxK

M3 - Article

AN - SCOPUS:0028814110

VL - 36

SP - 809

EP - 817

JO - Plant and Cell Physiology

JF - Plant and Cell Physiology

SN - 0032-0781

IS - 5

ER -