The Human COL11A2 Gene Structure Indicates that the Gene Has Not Evolved with the Genes for the Major Fibrillar Collagens
Open Access
- 1 September 1995
- journal article
- research article
- Published by Elsevier BV in Journal of Biological Chemistry
- Vol. 270 (39), 22873-22881
- https://doi.org/10.1074/jbc.270.39.22873
Abstract
The human COL11A2 gene was analyzed from two overlapping cosmid clones that were previously isolated in the course of searching the human major histocompatibility region (Janatipour, M., Naumov, Y., Ando, A., Sugimura, K., Okamoto, N., Tsuji, K., Abe, K., and Inoko, H.(1992) Immunogenetics 35, 272-278). Nucleotide sequencing defined over 28,000 base pairs of the gene. It was shown to contain 66 exons. As with most genes for fibrillar collagens, the first intron was among the largest, and the introns at the 5′-end of the gene were in general larger than the introns at the 3′-end. Analysis of the exons coding for the major triple helical domain indicated that the gene structure had not evolved with the genes for the major fibrillar collagens in that there were marked differences in the number of exons, the exon sizes, and codon usage. The gene was located close to the gene for the retinoic X receptor β in a head-to-tail arrangement similar to that previously seen with the two mouse genes (P. Vandenberg and D. J. Prockop, submitted for publication). Also, there was marked interspecies homology in the intergenic sequences. The amino acid sequences and the pattern of charged amino acids in the major triple helix of the α2(XI) chain suggested that the chain can be incorporated into the same molecule as α1(XI) and α1(V) chains but not into the same molecule as the α3(XI)/α1(II) chain. The structure of the carboxyl-terminal propeptide was similar to the carboxyl-terminal propeptides of the proα1(XI) chain and proα chains of other fibrillar collagens, but it was shorter because of internal deletions of about 30 amino acids.Keywords
This publication has 36 references indexed in Scilit:
- The α2(XI) procollagen transcript undergoes complex altenative splicing at the N-propeotide coding regionMatrix Biology, 1994
- Molecular cloning of PARP (proline/arginine‐rich protein) from human cartilage and subsequent demonstration that PARP is a fragment of the NH2‐terminal domain of the collagen α2(XI) chainFEBS Letters, 1993
- The human rhabdomyosarcoma cell line A204 lays down a highly insoluble matrix composed mainly of α1 type‐XI and α2 type‐V collagen chainsEuropean Journal of Biochemistry, 1992
- Search for MHC-associated genes in human: five new genes centromeric to HLA-DP with yet unknown functionsImmunogenetics, 1992
- THE FAMILY OF COLLAGEN GENESAnnual Review of Biochemistry, 1990
- Cartilage contains mixed fibrils of collagen types II, IX, and XI.The Journal of cell biology, 1989
- COOH-terminal propeptides of the major human procollagensJournal of Molecular Biology, 1987
- 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
- Minor collagens of chicken hyaline cartilageBiochemistry, 1981
- Collagen heterogeneity in human cartilage: Identification of several new collagen chainsBiochemical and Biophysical Research Communications, 1979