Deletion analysis of the dystrophin‐actin binding domain
Authors:
- P.L. MillsPMP.L. Mills
- J.S. ChamberlainJCJ.S. Chamberlain
- 16 May 1994
- journal article
- Published by Wiley in FEBS Letters
- Vol. 344 (2-3) , 255-260
Abstract
Three sequence motifs at the N‐terminus of dystrophin have previously been proposed to be important for binding to actin. By analyzing a series of purified bacterial fusion proteins deleted for each of these sites we have demonstrated that none of the three are critical for dystrophin‐actin interactions. Instead, our data suggest that sequences in the N‐terminal 90 amino acids of dystrophin, excluding a conserved KTFT motif, contain the major site for interaction with actin.Keywords
This publication has 26 references indexed in Scilit:
- Actin-dystrophin interfaceBiochemistry, 1993
- A B2 Repeat Insertion Generates Alternate Structures of the Mouse Muscle γ-Phosphorylase Kinase GeneGenomics, 1993
- Interaction of Dystrophin with Cytoskeletal Proteins: Binding to Talin and ActinBiochemical and Biophysical Research Communications, 1993
- The identification and characterisation of an actin‐binding site in α‐actinin by mutagenesisFEBS Letters, 1992
- Expression of the N‐terminal domain of dystrophin in E. coli and demonstration of binding to F‐actinFEBS Letters, 1992
- Binding sites involved in the interaction of actin with the N‐terminal region of dystrophinFEBS Letters, 1992
- Nebulin as a giant actin‐binding template protein in skeletal muscle sarcomere Interaction of actin and cloned human nebulin fragmentsFEBS Letters, 1991
- Expression of recombinant dystrophin and its localization to the cell membraneNature, 1991
- The interaction of actin with dystrophinFEBS Letters, 1990
- Very mild muscular dystrophy associated with the deletion of 46% of dystrophinNature, 1990