Journal article
Can calmodulin function without binding calcium?
Cell (Cambridge), Vol.65(6), pp.949-959
1991
Handle:
https://hdl.handle.net/2376/115990
PMID: 2044154
Abstract
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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Details
- Title
- Can calmodulin function without binding calcium?
- Creators
- John R GeiserDiederik van TuinenSusan E BrockerhoffMichael M NeffTrisha N Davis
- Publication Details
- Cell (Cambridge), Vol.65(6), pp.949-959
- Academic Unit
- Crop and Soil Sciences, Department of
- Publisher
- Elsevier Inc
- Identifiers
- 99900547780001842
- Language
- English
- Resource Type
- Journal article