Interaction of tubulin with phospholipid vesicles. II. Physical changes of the protein.

  • Kumar N
  • Klausner R
  • Weinstein J
 et al. 
  • 1


    Mendeley users who have this article in their library.
  • N/A


    Citations of this article.


We have shown that soluble tubulin will bind to small unilamellar vesicles of dipalmitoyl phosphatidylcholine (Klausner, R. D., Kumar, N., Weinstein, J. N., Blumenthal, R., and Flavin, M. (1981) J. Biol. Chem. 256, 5879-5885). This association uniquely occurs at the lipid phase transition. The tubulin, when bound to the vesicles, displays an altered tryptophan fluorescence characterized by a 5-nm blue shift in the emission maximum and a 22% decrease in fluorescence intensity, when compared to soluble tubulin. Tryptophans in vesicle-bound tubulin are less accessible to the aqueous collisional quenchers, acrylamide and iodide, than in soluble tubulin. Circular dichroism studies reveal an increase in alpha-helical content of tubulin as a result of vesicle interaction. Proteolytic digestion by trypsin of vesicle bound tubulin is slower than of soluble tubulin. The beta subunit of tubulin is preferentially protected from trypsin by vesicle interaction. Furthermore, the pattern of tryptic cleavage products is altered by this interaction.

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document


  • N. Kumar

  • R.D. Klausner

  • J.N. Weinstein

  • R. Blumenthal

  • M. Flavin

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free