The interaction between subunits in the tubulin dimer.

Abstract

Limited proteolysis and chemical cross-linking techniques have been used to study the interaction between alpha- and beta-tubulin subunits. Trypsin digestion of tubulin dimer resulted in the cleavage of the alpha-subunit into two fragments, whereas chymotrypsin cleaved the beta-subunit into two distinct fragments. All of these fragments have been mapped on the tubulin subunits by further proteolysis with formic acid. Cross-linking of trypsin- and chymotrypsin-cleaved subunits has been performed with two different cross-linker agents of different cross-linking distance. The addition of formaldehyde resulted in the cross-linking of the alpha-tubulin N-terminal fragment with beta-tubulin C-terminal domain. The same result was obtained when methyl 4-mercaptobutyrimidate was used.

Cite this paper

@article{Serrano1985TheIB, title={The interaction between subunits in the tubulin dimer.}, author={Luis Serrano and Jes{\'u}s {\'A}vila}, journal={The Biochemical journal}, year={1985}, volume={230 2}, pages={551-6} }