Structure of a full-length cDNA clone for the preproα2(I) chain of human type I procollagen. Comparison with the chicken gene confirms unusual patterns of gene conservation
- 15 June 1988
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 252 (3), 633-640
- https://doi.org/10.1042/bj2520633
Abstract
A cDNA clone from a human placental library was found to consist of an essentially full-length cDNA of 4.6 kb for the prepro alpha 2(I) chain of type I procollagen. Nucleotide sequencing of the 5′-end of the cDNA provided a sequence of 1617 nucleotide residues and codons for 539 amino acid residues not previously defined. Comparison of the complete structure of the prepro alpha 2(I) cDNA with previously reported sequences for the chicken pro alpha 2(I) gene indicated that 83% of 1366 total amino acid residues were conserved. In the alpha-chain domain 84% of 1014 amino acid residues were conserved. Also, there was conservation of the previously noted preference for U and C in the third position of codons for glycine, proline and alanine. One major difference between the human and the chicken prepro alpha 2(I) chain was that the human chain contained 21 fewer proline residues, an observation that probably explains why the triple helix of human type I procollagen unfolds at temperatures that are 1-2 degrees C lower. In parallel experiments, sequencing of intron-exon boundaries for nine exons of genomic subclones confirmed and extended previous observations that the pro alpha 2(I) gene, like other genes from fibrillar collagens, has an unusual 54-base pattern of exon sizes that is highly conserved through evolution.This publication has 30 references indexed in Scilit:
- Nucleotide sequences of complementary deoxyribonucleic acids for the pro.alpha.1 chain of human type I procollagen. Statistical evaluation of structures that are conserved during evolutionBiochemistry, 1983
- Restriction fragment length polymorphism associated with the pro alpha 2(I) gene of human type I procollagen. Application to a family with an autosomal dominant form of osteogenesis imperfecta.JCI Insight, 1983
- Analysis of the 3' end of the human pro-alpha 2(I) collagen gene. Utilization of multiple polyadenylation sites in cultured fibroblasts.Journal of Biological Chemistry, 1983
- Structure of a cDNA for the pro.alpha.2 chain of human type I procollagen. Comparison with chick cDNA for pro.alpha.2(I) identifies structurally conserved features of the protein and the geneBiochemistry, 1983
- Isolation and characterization of overlapping genomic clones covering the chicken alpha 2 (type I) collagen gene.Proceedings of the National Academy of Sciences, 1980
- The collagen gene: Evidence for its evolutionary assembly by amplification of a DNA segment containing an exon of 54 bpCell, 1980
- Thermal stability of type I and type III procollagens from normal human fibroblasts and from a patient with osteogenesis imperfecta.Proceedings of the National Academy of Sciences, 1980
- Thermal stability of the triple helix of type I procollagen and collagen. Precautions for minimizing ultraviolet damage to proteins during circular dichroism studiesBiochemistry, 1979
- Covalent structure of collagen: amino acid sequence of chick skin collagen α1(I)-CB6BBiochemistry, 1978
- DNA sequencing with chain-terminating inhibitorsProceedings of the National Academy of Sciences, 1977