Demonstrates that the N-terminal domain of human dystrophin is a functionally competent actin-binding protein, confirming its role in binding F-actin.
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Confirms N-terminal dystrophin as functional F-actin binder; extends biochemical data but leaves open in vivo and therapeutic relevance.
The N-terminal head domain of human dystrophin has been expressed in soluble form and high yield in E. coli, allowing us to test the previously unconfirmed assumption that dystrophin binds actin. DMD246, the first 246 amino acid residues of dystrophin, binds F-actin in a strongly co-operative manner with a Hill constant of 3.5, but does not bind G-actin. Dystrophin heads are thus functionally competent actin-binding proteins. This result opens the way to identifying critical residues in the actin-binding site and encourages us that the other domains of dystrophin might also be treated as functionally autonomous modules, accessible to a similar approach.
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Way et al. (1992) studied this question.
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