Binding Site of Annexin XI on the Calcyclin Molecule

M. Watanabe, Y. Ando, Hiroshi Tokumitsu, H. Hidaka

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Abstract

We purified rabbit calcyclin of S100 family protein and a calcyclin associated protein which has proved to be a novel annexin, annexin XI. Using a co-precipitation assay of annexin XI with phospholipid, the binding site of annexin XI on calcyclin was examined. The peptide fragment of calcyclin, CNBr-3 (residues 1-57), digested with cyanogen bromide completely inhibited the interaction of native calcyclin with annexin XI, while CNBr-l (residues 83-90) and CNBr-2 (residues 58-82) did not affect the binding. We then constructed and expressed recombinant cDNAs for wild type and four different deletion mutants lacking N-terminal portions. The wild type (wt) and mt1 mutant lacking three amino acids from N-terminal bound to annexin XI with phosphatidylserine and Ca2+, whereas mt2, mt3 and mt4 with seven, twelve and eighteen amino acids deleted, respectively, did not bind to annexin XI. Moreover, the truncated mutant from residues 4 to 7 (mt5) decreased the binding capacity. These observations suggest that four amino acids (residues 4-7) at the N-terminal portion of calcyclin play an important role in the interaction of calcyclin with annexin XI.

Original languageEnglish
Pages (from-to)1376-1382
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume196
Issue number3
DOIs
Publication statusPublished - Nov 15 1993
Externally publishedYes

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ASJC Scopus subject areas

  • Molecular Biology
  • Biophysics
  • Biochemistry

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