Key result
The V266G/L267G mutation in yeast actin lowered the melting temperature for Mg-GG actin from 51 to 33°C and transformed the conformation of subdomain 2 and the central cleft into an F-monomer-like structure.
Population
Yeast G-actin
Comparison
V266G/L267G mutation in the subdomain 3/4… vs Wild-type yeast G-actin
Design
Preclinical
Authors
Loading...
Highlights hydrophobic plug's role in actin stability; leaves open translation to mammalian or disease models.
Absolute Event Rate: 33% vs 51%
The hydrophobic plug in yeast G-actin is important for controlling monomer stability and promoting conformational changes needed for filament addition.
Kuang et al. (1997) studied Yeast G-actin mutation. V266G/L267G mutation vs. Wild-type actin was evaluated on Melting temperature for Mg-actin (°C). The V266G/L267G mutation in yeast actin lowered the melting temperature for Mg-GG actin from 51 to 33°C and transformed the conformation of subdomain 2 and the central cleft into an F-monomer-like structure.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: