Amino acid sequence of a novel calmodulin from Paramecium tetraurelia that contains dimethyllysine in the first domain

W. H. Schaefer, T. J. Lukas, I. A. Blair, J. E. Schultz, D. M. Watterson

Research output: Contribution to journalArticle

42 Scopus citations

Abstract

A class of Paramecium behavioral mutants called pantophobiacs have a deficiency in calcium-dependent potassium efflux, and this deficiency can be corrected by the microinjection of wild-type Paramecium calmodulin. As a starting point in investigations of which features allow wild-type Paramecium calmodulin to fully restore this behavior while other calmodulins are inactive or poorly effective, we elucidated the amino acid sequence of the wild-type calmodulin. We utilized an approach that combined Edman chemistry with mass spectrometry. This approach resulted in the identification of a new post-translational modification in calmodulin: N(ε),N(ε)-dimethyllysine at residue 13. This particular modification has not been described for calmodulins studied previously. The only other first-domain modification that has been described for any calmodulin is acetylation of the amino terminus. These results along with analyses of pantophobiac calmodulin and calmodulin binding proteins will provide insight into calmodulin's role in a well-defined behavioral mutant.

Original languageEnglish (US)
Pages (from-to)1025-1029
Number of pages5
JournalJournal of Biological Chemistry
Volume262
Issue number3
StatePublished - 1987

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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