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Substitution of cysteine for glycine alpha 1 691 in the proalpha 1i chain of type i procollagen in a proband with lethal osteogenesis imperfecta destabilizes the triple helix at a site carboxyl terminal to the substitution


Substitution of cysteine for glycine alpha 1 691 in the proalpha 1i chain of type i procollagen in a proband with lethal osteogenesis imperfecta destabilizes the triple helix at a site carboxyl terminal to the substitution



Biochemical Journal 279(3): 747-752



ISSN/ISBN: 0264-6021

Skin fibroblasts from a proband with lethal osteogenesis imperfecta synthesized a type I procollagen containing a cysteine residue in the .alpha.1(I) helical domain. Assay of thermal stability of the triple helix by proteinase digestion demonstrated a decreased temperature for thermal unfolding of the protein. Of special importance was the observation that assays of thermal stability by proteinase digestion revealed two bands present in a 2:1 ratio of about 140 and 70 kDa; the 140 kDa band was reducible to a 70 kDa band. Further analysis of the fragments demonstrated that the cysteine mutation produced a local unfolding of the triple helix around residue 700 and apparently exposed the arginine residue at position 704 in both the .alpha.1(I) and .alpha.2(I) chains. Analysis of cDNAs and genomic DNAs demonstrated a single-base mutation that changed the GGT codon for glycine-691 of the .alpha.1(I) chain to a TGT codon for cysteine. The mutation was not found in DNA from either of the proband's parents. Since the proteinase assay of helical stability generated a fragment of 700 residues that retained disulphide-bonded cysteine residues at .alpha.1-691, the results provide one of the first indications that glycine substitutions in type I procollagen can alter the conformation of the triple helix at a site that is C-terminal to the site of the substitution.

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Accession: 007842929

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Related references

Substitution of cysteine for glycine-alpha 1-691 in the pro alpha 1(I) chain of type I procollagen in a proband with lethal osteogenesis imperfecta destabilizes the triple helix at a site C-terminal to the substitution. Biochemical Journal 279: 747-752, 1991

Substitution of cysteine for glycine-1-691 in the pro1(I) chain of type I procollagen in a proband with lethal osteogenesis imperfecta destabilizes the triple helix at a site C -terminal to the substitution. Biochemical Journal 279(3): 747-752, 1991

Substitution of cysteine for glycine-α1-691 in the proα1(I) chain of type I procollagen in a proband with lethal osteogenesis imperfecta destabilizes the triple helix at a site C-terminal to the substitution. Biochemical Journal (London 1984) 279: 747-752, 1991

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A single base mutation that converts glycine 907 of the α2(I) chain of type I procollagen to aspartate in a lethal variant of osteogenesis imperfecta: the single amino acid substitution near the carboxyl terminus destabilizes the whole triple helix. The Journal of Biological Chemistry 264(5): 3002-3006, 1989

A single base mutation that converts glycine 907 of the a2(I) chain of type I procollagen to aspartate in a lethal variant of osteogenesis imperfecta. The single amino acid substitution near the carboxyl terminus destabilizes the whole triple helix. The Journal of Biological Chemistry 264: 02-6, 1989

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A point mutation in a type I procollagen gene converts glycine 748 of the a1 chain to cysteine and destabilizes the triple helix in a lethal variant of osteogenesis imperfecta. The Journal of Biological Chemistry 262: 737-44, 1987

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