Key result
The S14A mutation in yeast actin resulted in a 40-60-fold decrease in ATP affinity and decreased the apparent denaturation temperature for Ca-actin from 57 to 45 °C and Mg-actin from 52 to 40 °C.
Population
Saccharomyces cerevisiae G-actin (yeast actin)
Comparison
S14A mutation (conversion of Ser14 to Ala) vs Wild-type actin
Design
Preclinical
Authors
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Yeast actin S14A effects are hypothesis-generating; leaves open Ser14 relevance to mammalian cardiac actin stability.
The Ser14 hydroxyl in yeast actin forms a critical polar bridge with the ATP gamma-phosphate, conferring stability to the actin small domain and maintaining ATP affinity.
Chen et al. (1995) studied Saccharomyces cerevisiae G-Actin S14A mutation. S14A mutation vs. Wild-type actin was evaluated on Actin affinity for ATP and apparent denaturation temperature. The S14A mutation in yeast actin resulted in a 40-60-fold decrease in ATP affinity and decreased the apparent denaturation temperature for Ca-actin from 57 to 45 °C and Mg-actin from 52 to 40 °C.
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