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 in | Cell Vol. 47; no. 3; pp. 423 - 431 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
Cambridge, MA
Elsevier Inc
07.11.1986
Cell Press |
Subjects | |
Online Access | Get full text |
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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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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0092-8674 1097-4172 |
DOI: | 10.1016/0092-8674(86)90599-4 |