Inhibition of ATPase activity in pea plasma membranes by fungal suppressors from mycosphaerella pinodes and their peptide moieties

Toshiaki Kato, Tomonori Shiraishi, Kazuhiro Toyoda, Koji Saitoh, Yoshimi Satoh, Makoto Tahara, Tetsuji Yamada, Hachiro Oku

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

The effects of two suppressors of the defense reactions of host plants, which had been purified from the pea pathogen Mycosphaerella pinodes, as well as the effects of peptide moieties, on the ATPase activity in pea plasma membranes were examined in vitro. One of the suppressors, Supprescin B, inhibited the ATPase activity in a non-competitive manner, but the other suppressor, Supprescin A, did not. Supprescin A was observed to reduce the inhibitory effect of Supprescin B. A tripeptide, Ser-Ser-Gly, and a hexapeptide, Ser-Ser-Gly-Asp-Glu-Thr, which were the respective peptide moieties of Supprescin A and B, inhibited the ATPase activity in a competitive manner. Supprescin B and fragments of the hexapeptide, such as Asp-Glu-Thr and Gly- Asp-Glu, inhibited not only the ATPase activity but also the acid phosphatase activity of plasma membranes in vitro. These results indicate that the acidic amino-acid residues of the "Asp-Glu" moiety seem to act as inhibitors of the phosphatase activity. Thus, the peptide moiety of Supprescin B consists of at least two functional elements.

Original languageEnglish
Pages (from-to)439-445
Number of pages7
JournalPlant and Cell Physiology
Volume34
Issue number3
Publication statusPublished - Apr 1 1993

Keywords

  • ATPase
  • Mycosphaerella pinodes
  • Pisum sativum L.
  • Suppressor

ASJC Scopus subject areas

  • Physiology
  • Plant Science
  • Cell Biology

Fingerprint Dive into the research topics of 'Inhibition of ATPase activity in pea plasma membranes by fungal suppressors from mycosphaerella pinodes and their peptide moieties'. Together they form a unique fingerprint.

  • Cite this