Key result
The yeast actin mutant D56A/E57A increased the affinity of tropomyosin for actin 3-fold and decreased actin-myosin S1 affinity 13-fold in the presence of troponin-tropomyosin.
Population
Yeast actin mutant D56A/E57A and wild type actin
Comparison
Mutation D56A/E57A in actin subdomain 2 vs Wild type actin
Design
Preclinical
Authors
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Delineates key actin residues for thin filament regulation; leaves open relevance to human cardiac disease.
Negatively charged residues 56 and 57 in actin subdomain 2 are critical for myosin binding, tropomyosin-actin interactions, and regulatory conformational changes in the actin-troponin-tropomyosin complex.
Korman et al. (2000) studied this question. Yeast actin mutant D56A/E57A vs. Wild type actin was evaluated on Affinity of tropomyosin for actin and actin-myosin S1 affinity. The yeast actin mutant D56A/E57A increased the affinity of tropomyosin for actin 3-fold and decreased actin-myosin S1 affinity 13-fold in the presence of troponin-tropomyosin.
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