The complete sequence of dystrophin predicts a rod-shaped cytoskeletal protein

@article{Koenig1988TheCS,
  title={The complete sequence of dystrophin predicts a rod-shaped cytoskeletal protein},
  author={Michel Koenig and Anthony P. Monaco and Louis M. Kunkel},
  journal={Cell},
  year={1988},
  volume={53},
  pages={219-228}
}

An autosomal transcript in skeletal muscle with homology to dystrophin

THE Duchenne muscular dystrophy (DMD) gene has been localized to chromosome Xp211–6 and codes for a 14-kilobase (kb) transcript7 and a protein called dystrophin8, of relative molecular mass 427,000.

Spectrin-like repeats from dystrophin and alpha-actinin-2 are not functionally interchangeable.

A chimeric transgene containing the four-repeat rod domain of alpha-actinin-2 was expressed in mdx mice, and data demonstrated that different spectrin-like repeats are not equivalent, and reinforced the suggestion that the dystrophin rod domain is not merely a spacer but likely contributes an important mechanical role to overall dyStrophin function.

Spectrin-like repeats from dystrophin and α-actinin-2 are not functionally interchangeable

A chimeric transgene containing the four-repeat rod domain of alpha-actinin-2 was expressed in mdx mice, and data demonstrated that different spectrin-like repeats are not equivalent, and reinforced the suggestion that the dystrophin rod domain is not merely a spacer but likely contributes an important mechanical role to overall dyStrophin function.

From the spectrin gene to the assembly of the membrane skeleton.

Comparison of the deduced amino acid sequence shows that alpha-spectrin is well conserved in different species and that the human erythrocyte alpha-Spectrin is divergent.

Minimum folding unit of dystrophin rod domain.

It appears that the minimum unit capable of forming the native fold extends some residues into the adjoining sequence repeat, and the fragment of 119 residues forms a significantly more stable structure than that of 117, which was found that the critical length for folding was 117 residues.

Primary structure and domain organization of human alpha and beta adducin

The complete sequence of both subunits of human adducin, alpha (737 amino acids), and beta (726 amino acids) has been deduced by analysis of the cDNAs, suggesting evolution by gene duplication.
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References

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Erythrocyte spectrin is comprised of many homologous triple helical segments

The results suggest that most of the human erythrocyte spectrin molecule is comprised of homologous segments with a 106 amino acid length per segment, and that spectrin is not related to any other proteins whose sequence was known.

Subcellular fractionation of dystrophin to the triads of skeletal muscle

It is shown that dystrophin is associated with the triadic junctions in skeletal muscle, and is therefore probably involved with Ca2+ homoeostasis, and shown that the ∼450K ryanodine receptor/sarcoplasmic reticulum Ca1+ channel8, which has the large size and subcellular distribution characteristics of dyStrophin, is an immunologically distinct protein species.

Deletions of fetal and adult muscle cDNA in Duchenne and Becker muscular dystrophy patients.

It is demonstrated that a very mildly affected 61 year old patient is deleted for at least nine exons of the adult cDNA, suggesting that there must be less essential domains of the protein structure which can be removed without complete loss of function.

Isolation of candidate cDNAs for portions of the Duchenne muscular dystrophy gene

The nucleotide sequence of two highly conserved DNA fragments from the DXS164 locus and their homologous sequences from the mouse X chromosome are presented and are candidates for portions of the gene responsible for both DMD and BMD.

Conservation of the Duchenne muscular dystrophy gene in mice and humans.

A portion of the Duchenne muscular dystrophy (DMD) gene transcript from human fetal skeletal muscle and mouse adult heart was sequenced, suggesting that the protein product might serve a structural role in muscle, but the abundance and tissue distribution of the messenger RNA suggests that the DMD protein is not nebulin.

Periodic charge distributions in the myosin rod amino acid sequence match cross-bridge spacings in muscle

Calculations suggest that the N-terminal third of the rod is only loosely associated with the thick filament backbone and could be used to act as a hinged arm during muscle contraction.