Site-directed mutation makes rabbit calcyclin dimer

Yuhko Ando, Masato Watanabe, Hajime Akatsuka, Hiroshi Tokumitsu, Hiroyoshi Hidaka

Research output: Contribution to journalArticlepeer-review

8 Citations (Scopus)


Unlike human, rat and mouse calcyclin, purified rabbit calcyclin did not form a dimer on Tricine SDS-PAGE under non-reduced conditions. Based on the internal peptide sequence of rabbit calcyclin, we isolated and sequenced a cDNA clone encoding calcyclin. The sequence of this clone (pCaiC) is 629 bp long and codes 90 amino acid residues of a protein with a molecular mass of 10,153 Da. By Northern blot analysis, a major band of 0.9 kbp and a minor band of 2.6 kbp were detected in the lung. The recombinant calcyclin mutated serine at the third position to cysteine was expressed in E. coli and made dimer formation under non-reduced conditions on SDS-PAGE. Whether or not this type of mutation which prevents dimer formation of calcyclin plays a physiological role in the rabbit lung is the subject of an ongoing study.

Original languageEnglish
Pages (from-to)109-113
Number of pages5
JournalFEBS Letters
Issue number2
Publication statusPublished - Dec 14 1992
Externally publishedYes


  • Calcyclin
  • EF-hand protein
  • Expression of cDNA
  • cDNA cloning

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


Dive into the research topics of 'Site-directed mutation makes rabbit calcyclin dimer'. Together they form a unique fingerprint.

Cite this