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. 1977 Oct;74(10):4375-7.
doi: 10.1073/pnas.74.10.4375.

Interactions of a photoaffinity analog of GTP with the proteins of microtubules

R L Geahlen, B E Haley

Interactions of a photoaffinity analog of GTP with the proteins of microtubules

R L Geahlen et al. Proc Natl Acad Sci U S A. 1977 Oct.

Abstract

Tubulin dimers isolated from brain contain two GTP binding sites, a nonexchangeable site and an exchangeable site. To localize the exchangeable site, we used a photoaffinity analog of GTP, 8-azidoguanosine triphosphate (8-N3GTP), which supports 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 photo-incorporation of [beta, gamma-32P]8-N3GTP whereas preincubation with ATP did not.

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