Intragenic suppressors of Dictyostelium myosin G680 mutants provide insights into inaccessible conformations of the molecular motor.
No immediate clinical implications; leaves open validation of myosin conformational insights in mammalian models.
We are using intragenic suppression to generate inferences about currently inaccessible conformations of the molecular motor myosin. We identified 19 unique suppressors of Dictyostelium G680A and G680V mutants and find that they are structurally and chemically restricted, suggestive of specific, compensatory mechanisms of action. Suppressors cluster in two adjacent elements of the myosin structure, one of which is dominated by substitutions that increase the volume of hydrophobic residues. The suppressors outline a general model for the mechanism of suppression of the G680A and G680V alterations. Secondary phenotypes conferred by suppressors independent of the G680 changes demonstrate that they will be useful substrates for biochemical and genetic characterization.
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Bruce K. Patterson (1998) studied this question.
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