Can calmodulin function without binding calcium?
Calmodulin is a small Ca 2+-binding protein proposed to act as the intracellular Ca 2+ receptor that translates Ca 2+ signals into cellular responses. We have constructed mutant yeast calmodulins in which the Ca 2+-binding loops have been altered by site-directed mutagenesis. Each of the mutant prot...
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Published in | Cell Vol. 65; no. 6; pp. 949 - 959 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
Cambridge, MA
Elsevier Inc
14.06.1991
Cell Press Elsevier |
Subjects | |
Online Access | Get full text |
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Summary: | Calmodulin is a small Ca
2+-binding protein proposed to act as the intracellular Ca
2+ receptor that translates Ca
2+ signals into cellular responses. We have constructed mutant yeast calmodulins in which the Ca
2+-binding loops have been altered by site-directed mutagenesis. Each of the mutant proteins has a dramatically reduced affinity for Ca
2+; one does not bind detectable levels of
45Ca
2+ either during gel filtration or when bound to a solid support. Furthermore, none of the mutant proteins change conformation even in the presence of high Ca
2+ concentrations. Surprisingly, yeast strains relying on any of the mutant calmodulins not only survive but grow well. In contrast, yeast strains deleted for the calmodulin gene are not viable. Thus, calmodulin is required for growth, but it can perform its essential function without the apparent ability to bind Ca
2+. |
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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(91)90547-C |