The interaction of phomopsin A with bovine brain tubulin

Richard F. Ludueña, Veena Prasad, Mary Carmen Roach, Ernest Lacey

Research output: Contribution to journalArticle

39 Scopus citations

Abstract

Phomopsin A is an anti-mitotic compound from the fungus Phomopsis leptostromiformis which is a potent inhibitor of microtubule assembly in vitro; like maytansine, it is known to compete with vinblastine for binding to tubulin (E. Lacey, J. A. Edgar, and C. C. J. Culvenor (1987) Biochem. Pharmacol. 36, 2133-2138). A major difference between the effects of maytansine and vinblastine is that vinblastine is a potent inhibitor of tubulin decay, whereas maytansine has little or no effect on decay. Since phomopsin A is structurally distinct from either maytansine or vinblastine, tubulin decay may be measured by either the time-dependent loss of the ability to bind to [3H]colchicine or the time-dependent increase in the binding of bis(8-anilinonaphthalene 1-sulfonate) (BisANS) to tubulin. By either method, phomopsin A was found to be a much stronger inhibitor of tubulin decay than is vinblastine or any other drug yet tested, and, in fact, when decay is measured by the increase of BisANS binding, phomopsin A appears to stop the process entirely. This may prove to be useful in the determination of the higherorder structure of the tubulin molecule.

Original languageEnglish (US)
Pages (from-to)32-38
Number of pages7
JournalArchives of Biochemistry and Biophysics
Volume272
Issue number1
DOIs
StatePublished - Jul 1989

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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