Mechanism of inhibition of cytoplasmic streaming by a myosin inhibitor, 2,3-butanedione monoxime

M. Tominaga*, E. Yokota, S. Sonobe, T. Shimmen

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

59 Citations (Scopus)


On the basis of the inhibition of myosin by 2,3-butanedione monoxime (BDM), the protein's involvement in various cell activities is discussed. However, it has not been established whether BDM inhibits plant myosin. In the present study, the effect of BDM on isolated plant myosin was analyzed in vitro. The sliding between myosin from lily (Lilium longiflorum) pollen tubes and actin filaments from skeletal muscle was inhibited to 25% at a concentration of 60 mM, indicating that BDM can be used as a myosin inhibitor for plant materials. Cytoplasmic streaming was completely inhibited by BDM at 30 mM in lily pollen tubes and at 70 mM in short root hair cells, and at 100 mM in long root hair cells of Hydrocharis dubia. However, BDM at high concentrations induced the disorganization of actin filament bundles in lily pollen tubes and short root hair cells. In addition, cortical microtubules were also fragmented in short root hair cells treated with BDM, suggesting a possible side effect of BDM.

Original languageEnglish
Pages (from-to)46-54
Number of pages9
Issue number1-2
Publication statusPublished - 2000
Externally publishedYes


  • 2,3-Butanedione monoxime
  • Actin filament
  • Hydrocharis dubia
  • In vitro motility assay
  • Myosin
  • Pollen tube
  • Root hair cell

ASJC Scopus subject areas

  • Plant Science
  • Cell Biology


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