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In vitro expressed dystrophin fragments do not associate with each other
Author(s) -
Chan Yiu-mo,
Kunkel Louis M.
Publication year - 1997
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/s0014-5793(97)00454-7
Subject(s) - dystrophin , spectrin , utrophin , cytoskeleton , hylobates , duchenne muscular dystrophy , immunoprecipitation , microbiology and biotechnology , biology , muscular dystrophy , in vitro , actinin , chemistry , genetics , cell culture , cell , paleontology
Dystrophin, a component of the muscle membrane cytoskeleton, is the protein altered in Duchenne Muscular Dystrophy (DMD) and Becker Muscular Dystrophy (BMD). Dystrophin shares significant homology with other cytoskeletal proteins, such as α‐actinin and spectrin. On the basis of its sequence similarity with α‐actinin and spectrin, dystrophin has been proposed to function as dimer. However, the existence of both dimers and monomers have been observed by electron microscopy. To address this apparent discrepancy, we expressed dystrophin fragments composed of different domains in an in vitro translation system. The expressed fragments were tested for their ability to interact with each other and full‐length dystrophin by both immunoprecipitation and blot overlay assays. These assays were successfully used to demonstrate the dimerization of α‐actinin and spectrin, yet failed to detect any interaction between dystrophin fragments. Although these in vitro results do not prove that dystrophin is not a dimer in vivo, they do indicate that this interaction is not like that of the α‐actinin and spectrin.