The interaction between subunits in the tubulin dimer.
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.
D000818:Animals; D002918:Chymotrypsin; D003432:Cross-Linking Reagents; D004591:Electrophoresis, Polyacrylamide Gel; D005557:Formaldehyde; D007096:Imidoesters; D010446:Peptide Fragments / Q000032:analysis; D013381:Subtilisins; D013552:Swine; D014357:Trypsin; D014404:Tubulin
D003432:Cross-Linking Reagents; D007096:Imidoesters; D010446:Peptide Fragments; D014404:Tubulin; D005557:Formaldehyde; C005905:methyl 4-mercaptobutyrimidate; D013381:Subtilisins; D002918:Chymotrypsin; D014357:Trypsin