Title : Gain of function mutations for yeast calmodulin and calcium dependent regulation of protein kinase activity.

Pub. Date : 1994 Sep 29

PMID : 7918668






12 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Yeast calmodulin binds only three calcium ions in the presence of millimolar concentrations of magnesium due to a defective calcium-binding sequence in its carboxyl terminal domain. Calcium calmodulin Saccharomyces cerevisiae S288C
2 Yeast calmodulin binds only three calcium ions in the presence of millimolar concentrations of magnesium due to a defective calcium-binding sequence in its carboxyl terminal domain. Calcium calmodulin Saccharomyces cerevisiae S288C
3 Yeast calmodulin"s diminished calcium-binding activity can be restored to that of other calmodulins by the use of site-directed mutagenesis to substitute its fourth calcium-binding domain with that of a vertebrate calmodulin sequence. Calcium calmodulin Saccharomyces cerevisiae S288C
4 Yeast calmodulin"s diminished calcium-binding activity can be restored to that of other calmodulins by the use of site-directed mutagenesis to substitute its fourth calcium-binding domain with that of a vertebrate calmodulin sequence. Calcium calmodulin Saccharomyces cerevisiae S288C
5 Yeast calmodulin"s diminished calcium-binding activity can be restored to that of other calmodulins by the use of site-directed mutagenesis to substitute its fourth calcium-binding domain with that of a vertebrate calmodulin sequence. Calcium calmodulin Saccharomyces cerevisiae S288C
6 Yeast calmodulin"s diminished calcium-binding activity can be restored to that of other calmodulins by the use of site-directed mutagenesis to substitute its fourth calcium-binding domain with that of a vertebrate calmodulin sequence. Calcium calmodulin Saccharomyces cerevisiae S288C
7 However, the repair of yeast calmodulin"s calcium-binding activity is not sufficient to repair quantitatively yeast calmodulin"s defective protein kinase activator activity. Calcium calmodulin Saccharomyces cerevisiae S288C
8 Yeast calmodulin"s activator activity with smooth muscle and skeletal muscle myosin light chain kinases and brain calmodulin-dependent protein kinase II can be progressively repaired by additional substitutions of vertebrate calmodulin sequences, provided that the four calcium-binding sites remain intact. Calcium calmodulin Saccharomyces cerevisiae S288C
9 These and previous results indicate that the binding of four calcium ions by calmodulin is necessary but not sufficient to bring about quantitative activation of protein kinases, and are consistent with the conformational selection/restriction model of the dynamic equilibrium among calcium, calmodulin and each calmodulin regulated enzyme. Calcium calmodulin Saccharomyces cerevisiae S288C
10 These and previous results indicate that the binding of four calcium ions by calmodulin is necessary but not sufficient to bring about quantitative activation of protein kinases, and are consistent with the conformational selection/restriction model of the dynamic equilibrium among calcium, calmodulin and each calmodulin regulated enzyme. Calcium calmodulin Saccharomyces cerevisiae S288C
11 These and previous results indicate that the binding of four calcium ions by calmodulin is necessary but not sufficient to bring about quantitative activation of protein kinases, and are consistent with the conformational selection/restriction model of the dynamic equilibrium among calcium, calmodulin and each calmodulin regulated enzyme. Calcium calmodulin Saccharomyces cerevisiae S288C
12 These and previous results indicate that the binding of four calcium ions by calmodulin is necessary but not sufficient to bring about quantitative activation of protein kinases, and are consistent with the conformational selection/restriction model of the dynamic equilibrium among calcium, calmodulin and each calmodulin regulated enzyme. Calcium calmodulin Saccharomyces cerevisiae S288C