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Expression of the N‐terminal domain of dystrophin in E. coli and demonstration of binding to F‐actin
Author(s) -
Way M.,
Pope B.,
Cross R.A.,
Kendrick-Jones J.,
Weeds A.G.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80249-g
Subject(s) - dystrophin , actin , actin binding protein , binding domain , microbiology and biotechnology , domain (mathematical analysis) , binding site , chemistry , plasma protein binding , biology , biochemistry , biophysics , actin cytoskeleton , cytoskeleton , cell , gene , mathematical analysis , mathematics
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.