NDLI: The biphasic kinetics of Colchicine-Tubulin interaction : Role of amino acids surrounding the A-ring of bound colchicine molecule

Content Provider	PubMed Central
Author	Gupta, Suvroma Banerjee, Mithu Poddar, Asim Banerjee, Asok Basu, Gautam Roy, Debjani Bhattacharya, Bhabatarak
Abstract	Isotypes of vertebrate tubulin have variable amino acid sequences which are clustered at their C-terminal ends. Isotypes bind colchicine at different on-rates and affinity constants. The kinetics of colchicine binding to purified (unfractionated) brain tubulin have been reported to be biphasic under pseudo-first order conditions. Experiments with individual isotypes established that the presence of βIII in the purified tubulin is responsible for the biphasic kinetics. Since the isotypes mainly differ at the C-termini, the colchicine binding kinetics of unfractionated tubulin and the βIII isotype, cleaved at the C-termini, have been tested under pseudo-first order conditions. Removal of the C-termini made no difference to the nature of the kinetics. Sequence alignment of different β isotypes of tubulin showed that besides the C-terminal region, there are differences in the main body as well. In order to establish whether these differences lie at the colchicine binding site or not, homology modeling of all β tubulin isotypes was done. We found that the isotypes differed from each other in the amino acids located near the A-ring of colchicine at the colchicine-binding site on β-tubulin. While the βIII isotype has two hydrophilic residues (Serine242 and Threonine317) both βII and βIV have two hydrophobic residues (Leucine242 and Alanine317). βII has Isoleucine at position 318, while βIII and βIV have Valine at that position. Thus these alterations in the nature of the amino acids surrounding the colchicine site could be responsible for the different colchicine binding kinetics of the different isotypes of tubulin.
Related Links	http://dx.doi.org/10.1021/bi050599l
Ending Page	10188
Page Count	8
Starting Page	10181
File Format	PDF
ISSN	00062960
e-ISSN	15204995
Journal	Biochemistry
Issue Number	30
Volume Number	44
Language	English
Publisher Date	2005-08-01
Access Restriction	Open
Subject Keyword	Biochemistry Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Biochemistry

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