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Nemaline myopathies are diseases characterized by the presence in muscle fibres of pathognomonic rod bodies. These are composed largely of alpha-actinin and actin. We have identified a missense mutation in the alpha-tropomyosin gene, TPM3, which segregates completely with the disease in a family whose autosomal dominant nemaline myopathy we had previously localized to chromosome 1p13-q25. The mutation substitutes an arginine residue for a highly conserved methionine in a putative actin-binding site near the N terminus of the alpha-tropomyosin. The mutation may strengthen tropomyosin - actin binding, leading to rod body formation, by adding a further basic residue to the postulated actin-binding motif.

Original publication

DOI

10.1038/ng0195-75

Type

Journal article

Journal

Nat Genet

Publication Date

01/1995

Volume

9

Pages

75 - 79

Keywords

Amino Acid Sequence, Base Sequence, Chromosomes, Human, Pair 1, DNA, DNA Mutational Analysis, DNA Primers, Exons, Female, Genes, Dominant, Genetic Linkage, Humans, Male, Molecular Sequence Data, Myopathies, Nemaline, Pedigree, Point Mutation, Polymorphism, Genetic, Tropomyosin