Isolation of the yeast calmodulin gene: Calmodulin is an essential protein

Calmodulin was purified from Saccharomyces cerevisiae based on its characteristic properties. Like other calmodulins, the yeast protein is small, heat-stable, acidic, retained by hydrophobic matrices in a Ca 2+-dependent manner, exhibits a pronounced Ca 2+-induced shift in electrophoretic mobility,...

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Published inCell Vol. 47; no. 3; pp. 423 - 431
Main Authors Davis, Trisha N., Urdea, Mickey S., Masiarz, Frank R., Thorner, Jeremy
Format Journal Article
LanguageEnglish
Published Cambridge, MA Elsevier Inc 07.11.1986
Cell Press
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Summary:Calmodulin was purified from Saccharomyces cerevisiae based on its characteristic properties. Like other calmodulins, the yeast protein is small, heat-stable, acidic, retained by hydrophobic matrices in a Ca 2+-dependent manner, exhibits a pronounced Ca 2+-induced shift in electrophoretic mobility, and binds 45Ca 2+. Using synthetic oligonucleotide probes designed from the sequences of two tryptic peptides derived from the purified protein, the gene encoding yeast calmodulin was isolated. The gene (designated CMD1) is a unique, single-copy locus, contains no introns, and resides on chromosome II. The amino acid sequence of yeast calmodulin shares 60% identity with other calmodulins. Disruption or deletion of the yeast calmodulin gene results in a recessive-lethal mutation; thus, calmodulin is essential for the growth of yeast cells.
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ISSN:0092-8674
1097-4172
DOI:10.1016/0092-8674(86)90599-4