title: The human COL11A2 gene structure indicates that the gene has not evolved with the genes for the major fibrillar collagens.
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 beta 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 alpha 2(XI) chain suggested that the chain can be incorporated into the same molecule as alpha 1(XI) and alpha 1(V) chains but not into the same molecule as the alpha 3(XI)/alpha 1(II) chain. The structure of the carboxyl-terminal propeptide was similar to the carboxyl-terminal propeptides of the pro alpha 1(XI) chain and pro alpha chains of other fibrillar collagens, but it was shorter because of internal deletions of about 30 amino acids.
authors.affiliation: Department of Biochemistry and Molecular Biology, Jefferson Institute of Molecular Medicine, Jefferson Medical College, Thomas Jefferson University, Philadelphia, Pennsylvania 19107, USA.
authors.forename: M M
authors.initials: MM
authors.lastname: Vuristo
authors.forename: T
authors.initials: T
authors.lastname: Pihlajamaa
authors.forename: P
authors.initials: P
authors.lastname: Vandenberg
authors.forename: D J
authors.initials: DJ
authors.lastname: Prockop
authors.forename: L
authors.initials: L
authors.lastname: Ala-Kokko
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D005075:Biological Evolution; D003001:Cloning, Molecular; D003062:Codon; D003094:Collagen / Q000096:biosynthesis* / Q000737:chemistry / Q000235:genetics*; D003360:Cosmids; D017931:DNA Primers; D005091:Exons; D006801:Humans; D007438:Introns; D008285:Major Histocompatibility Complex; D051379:Mice; D008969:Molecular Sequence Data; D016133:Polymerase Chain Reaction; D011347:Procollagen / Q000737:chemistry / Q000235:genetics; D017433:Protein Structure, Secondary; D018168:Receptors, Retinoic Acid / Q000235:genetics; D047488:Retinoid X Receptors; D017386:Sequence Homology, Amino Acid; D012689:Sequence Homology, Nucleic Acid; D014157:Transcription Factors / Q000235:genetics
chemical_list: D003062:Codon; D017931:DNA Primers; D011347:Procollagen; D018168:Receptors, Retinoic Acid; D047488:Retinoid X Receptors; D014157:Transcription Factors; D003094:Collagen