Interactions of a photoaffinity analog of GTP with the proteins of microtubules.
- 1 October 1977
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 74 (10), 4375-4377
- https://doi.org/10.1073/pnas.74.10.4375
Abstract
Tubulin dimers isolated from brain [sheep] contain 2 GTP binding sites, a nonexchangeable site and an exchangeable site. To localize the exchangeable site, a photoaffinity analog of GTP, 8-azidoguanosine triphosphate (8-N3GTP), was used which supoorts tubulin polymerization in the absence of activating light. Photolysis of tubulin polymerized in the presence of 0.01 to 0.1 mM [.beta.,.gamma.-32P]8-N3GTP resulted in covalent incorporation of radioactivity only onto the .beta. monomer. Photolysis with 8-N3GTP also prevented any further repolymerization of the tubulin whereas like treatment in the presence of GTP had no effect. Preincubation of tubulin with GTP prevented photoincorporation of [.beta.,.gamma.-32P]8-N3GTP whereas preincubation with ATP did not.Keywords
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