Unknown

Dataset Information

0

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.

SUBMITTER: Serrano L 

PROVIDER: S-EPMC1152649 | biostudies-other | 1985 Sep

REPOSITORIES: biostudies-other

Similar Datasets

| S-EPMC3887213 | biostudies-literature
| S-EPMC6818183 | biostudies-literature
| S-EPMC5024590 | biostudies-literature
| S-EPMC7763485 | biostudies-literature
| S-EPMC2150673 | biostudies-literature
| S-EPMC3709894 | biostudies-literature
| S-EPMC2719563 | biostudies-literature
| S-EPMC3751744 | biostudies-literature
| S-EPMC3670325 | biostudies-literature
| S-EPMC5555654 | biostudies-literature