| Autor: |
D H, Cohn, S, Apone, D R, Eyre, B J, Starman, P, Andreassen, H, Charbonneau, A C, Nicholls, F M, Pope, P H, Byers |
| Rok vydání: |
1988 |
| Předmět: |
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| Zdroj: |
The Journal of biological chemistry. 263(29) |
| ISSN: |
0021-9258 |
| Popis: |
We have characterized a mutation that produces mild, dominantly inherited osteogenesis imperfecta. Half of the alpha 1 (I) chains of type I collagen synthesized by cells from an affected individual contain a cysteine residue in the 196-residue carboxyl-terminal cyanogen bromide peptide of the triple-helical domain (Steinmann, B., Nicholls, A., and Pope, F. M. (1986) J. Biol. Chem. 261, 8958-8964). Unexpectedly, sequence determined from a proteolytic fragment of the alpha 1 (I) chain derived from procollagen molecules synthesized in the presence of both [3H]proline and [35S]cysteine indicated that the cysteine is located at the third residue carboxyl-terminal to the triple-helical domain, normally a glycine. The nucleotide sequence of a fragment amplified from genomic DNA confirmed the location of the cysteine residue and showed that the mutation was a single nucleotide change in one COL1A1 allele. This represents a new class of mutations, point mutations outside the triple-helical domain of the chains of type I collagen, that produce the osteogenesis imperfecta phenotype. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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