Molecular and Cellular Biochemistry

, Volume 190, Issue 1, pp 47–54

A strange calmodulin of yeast

  • Michio Yazawa
  • Ken-ichi Nakashima
  • Koichi Yagi
Article

DOI: 10.1023/A:1006951710440

Cite this article as:
Yazawa, M., Nakashima, K. & Yagi, K. Mol Cell Biochem (1999) 190: 47. doi:10.1023/A:1006951710440

Abstract

Calmodulin of Saccharomyces cerevisiae has different Ca2+ binding properties from other calmodulins. We previously reported that the maximum number of Ca2+ binding was 3 mol/mol and the fourth binding site was defective, which was different from 4 mol/mol for others. Their macroscopic dissociation constants suggested the cooperative three Ca2+ bindings rather than a pair of cooperative two Ca2+ bindings of ordinary calmodulin. Here we present evidence for yeast calmodulin showing the intramolecular close interaction between the N-terminal half domain and the C-terminal half domain, while the two domains of ordinary calmodulin are independent of each other. We will discuss the relationship of the shape and the shape change caused by the Ca2+ binding to the enzyme activation in yeast. The functional feature of calmodulin in yeast will also be considered, which might be different from the one of vertebrate calmodulin.

calmodulinyeast calmodulinCa2+ bindingCa2+ binding proteinSaccharomyces cerevisiaeinterdomain interaction

Copyright information

© Kluwer Academic Publishers 1999

Authors and Affiliations

  • Michio Yazawa
    • 1
  • Ken-ichi Nakashima
    • 1
  • Koichi Yagi
    • 2
  1. 1.Division of Chemistry, Graduate School of ScienceHokkaido UniversitySapporoJapan
  2. 2.Agroscience Research LaboratoryHokkai Sankyo Co. Ltd.KitahiroshimaJapan