The Human COL11A2 Gene Structure Indicates that the Gene Has Not Evolved with the Genes for the Major Fibrillar Collagens
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, 272-2...
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Published in | The Journal of biological chemistry Vol. 270; no. 39; pp. 22873 - 22881 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
United States
American Society for Biochemistry and Molecular Biology
29.09.1995
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Subjects | |
Online Access | Get full text |
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Summary: | 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 5â²-end of the gene were
in general larger than the introns at the 3â²-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. |
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 |
ISSN: | 0021-9258 1083-351X |
DOI: | 10.1074/jbc.270.39.22873 |