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Substitution of serine for glycine 883 in the triple helix of the pro alpha 1 (I) chain of type I procollagen produces osteogenesis imperfecta type IV and introduces a structural change in the triple helix that does not alter cleavage of the molecule by procollagen N-proteinase


Substitution of serine for glycine 883 in the triple helix of the pro alpha 1 (I) chain of type I procollagen produces osteogenesis imperfecta type IV and introduces a structural change in the triple helix that does not alter cleavage of the molecule by procollagen N-proteinase



Journal of Biological Chemistry 269(48): 30352-30357



ISSN/ISBN: 0021-9258

PMID: 7982948

Type I procollagen secreted by dermal fibroblasts from an individual with osteogenesis imperfecta type IV was a mixture of normal molecules and molecules that were post-translationally overmodified. The individual was heterozygous for a G to A transition in the COL1A1 gene that resulted in the substitution of serine for glycine 883 in one or both of the pro alpha 1 (I) chains. The thermal stability of molecules containing overmodified chains was lower by 2 degrees C than that of normal molecules. However, following cleavage of the molecules with vertebrate collagenase, the temperature of denaturation of the overmodified A fragments (residues 1-775 of the helix did not contain the substitution) was 2 degrees C greater than that of A fragments from normal molecules. The rates of cleavage by procollogen N-proteinase (EC 3.4.214.14) (N-proteinase) of procollagen molecules in normal and osteogenesis imperfecta samples were not significantly different. The procollagen molecules in the osteogenesis imperfecta sample were also indistinguishable from those in control samples by rotary shadowing electron microscopy. The results suggest that this substitution of serine for glycine in the alpha 1 (I) chain of procollagen, like the substitution of aspartate for the same glycine previously described (Lightfoot, S. J., Holmes, D. F., Brass, A., Grant, M. E., Byers, P. H., and Kadler, K. E. (1992) J. Biol. Chem. 267, 25521-25528), can alter the structure of the triple helix N-terminal to the site of the substitution. However, in contrast to the aspartate for glycine substitution, the structural change is insufficient to delay the cleavage of the procollagen by N-proteinase and results in a mild rather than lethal phenotype.

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Accession: 047473776

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Related references

Substitution of serine for glycine 883 in the triple helix of the proa1(I) chain of type I procollagen produces osteogenesis imperfecta type IV and introduces a structural change in the triple helix that does not alter cleavage of the molecule by procollagen N-proteinase. The Journal of Biological Chemistry 269: 352-7, 1994

Substitutions for glycine alpha 1-637 and glycine alpha 2-694 of type I procollagen in lethal osteogenesis imperfecta. The conformational strain on the triple helix introduced by a glycine substitution can be transmitted along the helix. Journal of Biological Chemistry 266(24): 15608-15613, 1991

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 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, 1991

A tripeptide deletion in the triple-helical domain of the pro alpha 1(I) chain of type I procollagen in a patient with lethal osteogenesis imperfecta does not alter cleavage of the molecule by N-proteinase. Journal of Biological Chemistry 267(35): 25529-25534, 1992

Substitution of serine for alpha 1(I)-glycine 844 in a severe variant of osteogenesis imperfecta minimally destabilizes the triple helix of type I procollagen. The effects of glycine substitutions on thermal stability are either position of amino acid specific. Journal of Biological Chemistry 264(33): 19694-19699, 1989

Substitutions for glycine a1-637 and glycine a2-694 of type I procollagen in lethal osteogenesis imperfecta. The conformational strain on the triple helix introduced by a glycine substitution can be transmitted along the helix. The Journal of Biological Chemistry 266: 608-13, 1991

Substitutions for glycine α1-637 and glycine α2-694 of type I procollagen in lethal osteogenesis imperfecta : the conformational strain on the triple helix introduced by a glycine substitution can be transmitted along the helix. The Journal of Biological Chemistry 266(24): 15608-15613, 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

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 serine for a1(I)-glycine 844 in a severe variant of osteogenesis imperfecta minimally destabilizes the triple helix of type I procollagen. The effects of glycine substitutions on thermal stability are either position or amino acid specific. The Journal of Biological Chemistry 264: 694-9, 1989

Substitution of serine for α1(I)-glycine 844 in a severe variant of osteogenesis imperfecta minimally destabilizes the triple helix of type I procollagen: the effects of glycine substitutions on thermal stability are either position or amino acid specific. The Journal of Biological Chemistry 264(33): 19694-19699, 1989

A tripeptide deletion in the triple-helical domain of the Proα1(I) chain of type I procollagen in a patient with lethal osteogenesis imperfecta does not alter cleavage of the molecule by N-proteinase. The Journal of Biological Chemistry 267(35): 25529-25534, 1992

A tripeptide deletion in the triple-helical domain of the proa1(I) chain of type I procollagen in a patient with lethal osteogenesis imperfecta does not alter cleavage of the molecule by N-proteinase. The Journal of Biological Chemistry 267: 529-34, 1992

A point mutation in a type I procollagen gene converts glycine 748 of the alpha 1 chain to cysteine and destabilizes the triple helix in a lethal variant of osteogenesis imperfecta. Journal of Biological Chemistry 262(30): 14737-14744, 1987