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Involvement of colchicine binding site of tubulin in the polymerisation process
Author(s) -
Dasgupta D.,
Rajgopalan R.,
Gurnani S.
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80491-8
Subject(s) - lysine , tubulin , colchicine , residue (chemistry) , binding site , chemistry , methionine , microtubule , amino acid , polymerization , biochemistry , stereochemistry , biology , organic chemistry , microbiology and biotechnology , genetics , polymer
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‐amino groups of lysine residues of tubulin are shared by both the colchicine binding site and the polymerisation process.