The Protein Journal

, Volume 25, Issue 4, pp 250–256

Functional Contribution of Ca2+ and Mg2+ to the Intermolecular Interaction of Visinin-like Proteins

Authors

  • Feng-Fin Jheng
    • Institute of Biomedical SciencesNational Sun Yat-Sen University
  • Likuan Wang
    • Institute of Biomedical SciencesNational Sun Yat-Sen University
  • Liya Lee
    • Institute of Biomedical SciencesNational Sun Yat-Sen University
    • Institute of Biomedical SciencesNational Sun Yat-Sen University
OriginalPaper

DOI: 10.1007/s10930-006-9008-5

Cite this article as:
Jheng, F., Wang, L., Lee, L. et al. Protein J (2006) 25: 250. doi:10.1007/s10930-006-9008-5

The interaction of human visinin-like protein 1 (VILIP1) and visinin-like protein 3 (VILIP3) with divalent cations (Mg2+, Ca2+, Sr2+ and Ba2+) was explored using circular dichroism and fluorescence measurement. These results showed that the four cations each induced a different subtle change in the conformation of VILIPs. Moreover, VILIP1 and VILIP3 bound with Ca2+ or Mg2+ in a cooperative manner. Studies on the truncated mutants showed that the intact EF-3 and EF-4 were essential for the binding of VILIP1 with Ca2+ and Mg2+. Pull-down assay revealed that Ca2+ and Mg2+ enhanced the intermolecular interaction of VILIPs, and led to the formation of homo- and hetero-oligomer of VILIPs. Together with previous findings that Ca2+-dependent localization of VILIPs may be involved in the regulation of distinct cascades and deprivation of Ca2+-binding capacity of VILIPs did not completely eliminate their activity, it is likely to reflect that Mg2+-bound VILIPs may play a role in regulating the biological function of VILIPs in response to a concentration fluctuation of Ca2+ in cells.

Key words

Conformational changeintermolecular interactionmetal-bindingVILIP

Abbreviations:

ANS

8-Anilinonaphthalene-1-sulfonate

VILIP

Visinin-like protein

Copyright information

© Springer Science+Business Media, Inc. 2006