Involvement of colchicine binding site of tubulin in the polymerisation process

Abstract

Role of lysine residues in the colchicine binding site and in the assembly-disassembly process was examined. It was observed that at 4°C (pH 7.5-8, 8±1) lysine residues and the N-terminal methionine residue of tubulin were all buried within the molecule. Evidence indicates that ε{lunate}-amino groups of lysine residues of tubulin are shared by both the colchicine binding site and the polymerisation process. © 1983.

Publication Title

FEBS Letters

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