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Volume 270, Number 35, Issue of September 01, pp. 20235-20238, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Characterization of the Taxol Binding Site on the Microtubule
2-(m-AZIDOBENZOYL)TAXOL PHOTOLABELS A PEPTIDE (AMINO ACIDS 217-231) of beta-TUBULIN

(Received for publication, May 12, 1995; and in revised form, June 28, 1995)

Srinivasa Rao ,&nbsp;<WBR> George A. Orr ,&nbsp;<WBR> Ashok G. Chaudhary ,&nbsp;<WBR> David G. I. Kingston ,&nbsp;<WBR> Susan Band Horwitz

Photoaffinity labeling methods are being used to define the molecular contacts between taxol and its target protein, tubulin. Our laboratory has demonstrated previously that [^3H]3`-(p-azidobenzamido)taxol photolabels the N-terminal 31 amino acids of beta-tubulin (Rao, S., Krauss, N. E., Heerding, J. M., Swindell, C. S., Ringel, I., Orr, G. A., and Horwitz, S. B.(1994) J. Biol. Chem. 269, 3132-3134). The interaction of a second photoaffinity analogue of taxol, [^3H]2-(m-azidobenzoyl)taxol, with tubulin has been investigated. This analogue specifically photolabels beta-tubulin and the photolabeling is competed by both taxol and unlabeled 2-(m-azidobenzoyl)taxol indicating a common binding domain. To identify the site(s) of photoincorporation, [^3H]2-(m-azidobenzoyl)taxol-photolabeled beta-tubulin was subjected to sequential cyanogen bromide and tryptic digestions. Radiolabeled peptides were purified by reverse phase high performance liquid chromatography, and amino acid sequencing studies identified a peptide containing amino acid residues 217-231 of beta-tubulin as the major photolabeled domain.



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