Journal of Biomolecular NMR

, Volume 23, Issue 4, pp 323–324

Letter to the Editor: 1H, 15N and 13C resonance assignments of yeast Saccharomyces cerevisiaecalmodulin in the Ca2+-free state

Authors

  • Hiroaki Ishida
    • Divisions of Biological Sciences, Graduate School of ScienceHokkaido University
  • Ken-ichi Nakashima
    • Divisions of Biological Sciences, Graduate School of ScienceHokkaido University
  • Yasuhiro Kumaki
    • High Resolution NMR Laboratory, Graduate School of ScienceHokkaido University
  • Mitsuo Nakata
    • Divisions of Biological Sciences, Graduate School of ScienceHokkaido University
  • Kunio Hikichi
    • Chemistry, Graduate School of ScienceHokkaido University
    • Chemistry, Graduate School of ScienceHokkaido University
Article

DOI: 10.1023/A:1020230712212

Cite this article as:
Ishida, H., Nakashima, K., Kumaki, Y. et al. J Biomol NMR (2002) 23: 323. doi:10.1023/A:1020230712212

Abstract

Calmodulin (CaM) is a small Ca2+-binding protein, which has been found in all of eucaryotic cells examined. CaMs isolated from various species have highly conserved amino acid sequence (more than 90% identical), and show the same biological functions. CaM isolated from the baker's yeast (Saccharomyces cerevisiae) (yCaM), however, shares only 60% identity in the amino acid sequence with CaM from vertebrate, and shows quite distinct conformational and biochemical properties compared with those of CaM from other species. The conformational details of yCaM, however, have not been revealed yet. We achieved the chemical shift assignments of yCaM (146 amino acids) in the apo-state using uniformly 15N- and 13C-labeled protein. Consequently, the resonances of 95% atoms in the backbone amides were successfully assigned.

calmodulinchemical shift assignmentsyeast
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Copyright information

© Kluwer Academic Publishers 2002