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Science 18 February 1994:
Vol. 263. no. 5149, pp. 963 - 966
DOI: 10.1126/science.8310294
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Articles

Science, Vol 263, Issue 5149, 963-966
Copyright © 1994 by American Association for the Advancement of Science

articles

Diverse essential functions revealed by complementing yeast calmodulin mutants

Y Ohya and D Botstein

Department of Genetics, Stanford University School of Medicine, CA 94305.

Calmodulin, a cytoplasmic calcium-binding protein, is indispensable for eukaryotic cell growth. Examination of 14 temperature-sensitive yeast mutants bearing one or more phenylalanine to alanine substitutions in the single essential calmodulin gene of yeast (CMD1) revealed diverse essential functions. Mutations could be classified into four intragenic complementation groups. Each group showed different characteristic functional defects in actin organization, calmodulin localization, nuclear division, or bud emergence. Phenylalanine residues implicated in calmodulin localization and nuclear division are located in the amino-terminal half of the protein, whereas those implicated in actin organization and bud emergence are located in the carboxyl-terminal half.


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