FEBS Letters
Volume 581, Issue 26 , Pages 5019-5023, 30 October 2007

Differential colchicine-binding across eukaryotic families: The role of highly conserved Pro268β and Ala248β residues in animal tubulin

Edited by Michael R. Bubb

  • Mithu Banerjee

      Affiliations

    • Department of Biochemistry, Bose Institute, P-1/12 CIT Scheme VIIM, Kolkata 700 054, India
    • ,
  • Debjani Roy

      Affiliations

    • Bioinformatics Centre, Bose Institute, P-1/12 CIT Scheme VIIM, Kolkata 700 054, India
    • ,
  • B. Bhattacharyya

      Affiliations

    • Department of Biochemistry, Bose Institute, P-1/12 CIT Scheme VIIM, Kolkata 700 054, India
    • ,
  • Gautam Basu

      Affiliations

    • Department of Biophysics, Bose Institute, P-1/12 CIT Scheme VIIM, Kolkata 700 054, India
    • Corresponding Author InformationCorresponding author. Fax: +91 33 2355 3886.

Received 1 August 2007; received in revised form 13 September 2007; accepted 18 September 2007. published online 28 September 2007.

Abstract 

Colchicine–tubulin interaction, responsible for the disruption of microtubule formation, has immense pharmacological importance but is poorly understood in terms of its biological significance. The interaction is characterized by a marked higher affinity of colchicine for animal tubulins compared to tubulins from plants, fungi and protists. From an analysis of tubulin sequences and colchicine–tubulin crystal structure, we propose that Pro268β and Ala248β (270β and 250β in the crystal structure 1SA0) in animal tubulin are crucial for the observed differential binding. We also suggest that mediated by the binding of endogenous molecules to the colchicine-binding site, microtubule assembly in eukaryotes may be modulated in a family specific manner.

Abbreviations: PBS, primary colchicine-binding site, DC, DAMA-colchicine, EBS, extended colchicine-binding site, PCA, principal component analysis

Keywords: Tubulin, Colchicine, Binding site, Principal component analysis, Proline, Beta-strand

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PII: S0014-5793(07)01029-0

doi:10.1016/j.febslet.2007.09.047

FEBS Letters
Volume 581, Issue 26 , Pages 5019-5023, 30 October 2007

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