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Localization of the exchangeable nucleotide binding domain in beta-tubulin

Journal Article · · Biochem. Biophys. Res. Commun.; (United States)
Limited proteolysis of tubulin by alpha-chymotrypsin cleaved the beta-subunit preferentially at Tyr 281, generating primarily 35 kD and 17 kD fragments which were located in the amino terminal and the carboxy terminal regions, respectively. A small amount of a 19 kD fragment from the C-terminal end was also produced. Alpha-Chymotrypsin-treated tubulin retained the ability to exchange GTP and covalently incorporate nucleotide by direct photoaffinity labeling. SDS-PAGE and autoradiography analysis of the (alpha-/sup 32/P) GTP-labeled alpha-CT-treated tubulin showed that the 35 kD fragment was almost exclusively labeled, indicating that the exchangeable GTP binding domain resides in the amino terminal region of the beta-subunit.
Research Organization:
Univ. of Kansas, Lawrence
OSTI ID:
5531970
Journal Information:
Biochem. Biophys. Res. Commun.; (United States), Journal Name: Biochem. Biophys. Res. Commun.; (United States) Vol. 3; ISSN BBRCA
Country of Publication:
United States
Language:
English