| First Author | Sztrolovics R | Year | 1994 |
| Journal | Matrix Biol | Volume | 14 |
| Issue | 1 | Pages | 9-19 |
| PubMed ID | 8061924 | Mgi Jnum | J:20775 |
| Mgi Id | MGI:68844 | Doi | 10.1016/0945-053x(94)90025-6 |
| Citation | Sztrolovics R, et al. (1994) Identification of type I collagen gene polymorphisms: tolerance of sequence variation at an alpha 2(I) helix Y position. Matrix Biol 14(1):9-19 |
| abstractText | This study has examined the frequency and distribution of polymorphisms in the type I collagen coding sequences. RNA from a group of human skin fibroblast cell lines was analyzed by the chemical cleavage mismatch detection method using hydroxylamine, a reagent specific for C-base mismatches, and overlapping cDNA probes covering the entire prepro alpha 1(I) and prepro alpha 2(I) coding regions. Mismatches were detected at only two nucleotide positions, one in each of the type I collagen sequences, suggesting that polymorphisms are relatively rare within these cDNAs. cDNA sequence analysis demonstrated that the prepro alpha 1(I) mismatch, detected in only one cell line, was due to a sequence polymorphism involving the wobble position of the codon for arginine residue 59 within the amino-propeptide globular subdomain of the pro alpha 1(I) chain and not resulting in a change in the polypeptide primary structure. In contrast, the prepro alpha 2(I) mismatch, detected in 6 of the 16 cell lines, was shown to arise from a sequence polymorphism affecting the identity of Y-position residue 459 of the alpha 2(I) triple helical domain, resulting in an alanine/proline dimorphism at this position. This study is the first to identify a type I collagen coding sequence polymorphism resulting in an alteration at the level of the amino acid sequence. The data suggest that at least some alpha 1(I) and alpha 2(I) helix Y positions may be tolerant of sequence variation, particularly if the replacing amino acid is proline, a residue involved in stabilizing the collagen triple helix. |
