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Direct photoaffinity labeling of cysteine 211 or a nearby amino acid residue of beta-tubulin by guanosine 5 '-diphosphate bound in the exchangeable site

  1. Author:
    Bai, R. L.
    Ewell, J. B.
    Nguyen, N. Y.
    Hamel, E.

  2. Author Address

    Hamel E NIH, Lab Drug Discovery Res & Dev Bldg 37,Rm 5D02,37 Convent Dr Bethesda, MD 20892 USA NCI, Frederick Canc Res & Dev Ctr, Sci Applicat Int Corp, NIH Frederick, MD 21702 USA US FDA, Ctr Biol Evaluat & Res, Facil Biotechnol Resources Bethesda, MD 20892 USA NCI, Frederick Canc Res & Dev Ctr, Lab Drug Discovery Res & Dev,NIH, Dev Therapeut Program,Div Canc Treatment & Diag Frederick, MD 21702 USA
    1. Year: 1999
  2. Journal: Journal of Biological Chemistry
    1. 274
    2. 18
    3. Pages: 12710-12714
  4. Type of Article: Article
  1. Abstract:

    Tubulin with [8-C-14]GDP bound in the exchangeable site was exposed to ultraviolet light, and radiolabel was cross-linked to two peptide regions of the beta-subunit. Following enrichment for peptides cross-linked to guanosine by boronate chromatography, we confirmed that the cysteine 12 residue was the major site of crosslinking. However, significant radiolabel was also incorporated into a peptide containing amino acid residues 206 through 224. Although every amino acid in this peptide except cysteine 211 was identified by sequential Edman degradation, implying that this was the amino acid residue cross-linked to guanosine, radiolabel at C-8 was usually lost during peptide processing (probably during chromatography at pH 10). Consequently, the radiolabeled amino acid could not be unambiguously identified. [References: 17]

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