J. Biol. Chem., Vol. 262, Issue 3, 1025-1029, 01, 1987
Amino acid sequence of a novel calmodulin from Paramecium tetraurelia that contains dimethyllysine in the first domain
WH Schaefer, TJ Lukas, IA Blair, JE Schultz and DM Watterson
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
(Hinrichsen, R. D., Burgess-Cassler, A., Soltvelt, B. C., Hennessey, T.,
and Kung, C. (1986) Science 232, 503-506). 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 epsilon,N
epsilon-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 (Watterson, D. M., Sharief, F., and
Vanaman, T. C. (1980) J. Biol. Chem. 255, 962-975). 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.
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