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Related Experiment Videos

Actin-depolymerizing effect of dimeric macrolides, bistheonellide A and swinholide A

S Y Saito1, S Watabe, H Ozaki

  • 1Department of Veterinary Pharmacology, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Yayoi 1-1-1, Bunkyo-ku, Tokyo 113.

Journal of Biochemistry
|May 21, 1998
PubMed
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Dimeric marine toxins, bistheonellide A and swinholide A, inhibit actin polymerization by binding to G-actin. Bistheonellide A sequesters G-actin, while swinholide A shows weaker F-actin severing activity.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Marine Natural Products Chemistry

Background:

  • Actin polymerization is crucial for cellular processes.
  • Marine toxins like mycalolide B and aplyronine A are known to affect actin dynamics.
  • Dimeric marine toxins, bistheonellide A and swinholide A, share structural similarities with known actin-binding agents.

Purpose of the Study:

  • To compare the effects of bistheonellide A and swinholide A on actin polymerization.
  • To elucidate the mechanism of action of these dimeric marine toxins on actin.
  • To investigate the interaction of these toxins with actin and myosin.

Main Methods:

  • Monitoring pyrenyl-actin polymerization using fluorescence intensity.
  • SDS-PAGE to assess the interaction of toxin-actin complexes with myosin.

Related Experiment Videos

  • Measurement of nucleotide exchange rates in G-actin.

    • Main Results:

    • Bistheonellide A inhibited G-actin polymerization and induced F-actin depolymerization concentration-dependently.
    • One molecule of bistheonellide A binds two molecules of G-actin.
    • Toxin-bound G-actin complexes did not interact with myosin.
    • Bistheonellide A showed irreversible depolymerizing effects and increased nucleotide exchange.
    • Swinholide A exhibited weaker F-actin severing activity than mycalolide B.

    Conclusions:

    • Bistheonellide A inhibits actin polymerization by sequestering G-actin through a tertiary complex formation.
    • Different conformational changes in actin are induced by bistheonellide A and swinholide A.
    • Structural differences in side chains may explain variations in severing activity among dimeric macrolides.