ISOLATION OF CDNAS ENCODING THE COMPLETE SEQUENCE OF BOVINE TYPE-X COLLAGEN - EVIDENCE FOR THE CONDENSED NATURE OF MAMMALIAN TYPE-X COLLAGEN GENES

被引:49
|
作者
THOMAS, JT
KWAN, APL
GRANT, ME
BOOTHANDFORD, RP
机构
[1] Department of Biochemistry, School of Biological Sciences, University of Manchester, Manchester M13 9PT, Oxford Road
关键词
D O I
10.1042/bj2730141
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The complete primary structure of the bovine alpha-1(X) collagen chain was determined by nucleotide sequencing of cDNA clones. The overlapping cDNA clones encode 3144 bp with a 5'-terminal untranslated region of 148 bp, a 2025 bp reading frame and a 3'-terminal untranslated region of 971 bp. This represents the first complete sequence of a mammalian type X collagen cDNA and has allowed a number of informative comparisons to be made with the previously published chick alpha-1(X) sequence. The primary translation products of both bovine and chick type X collagen are 674 amino acid residues in length and there is a 73.3 % identity at the amino acid level (67.8 % at the base level). Sequence analyses reveal that the greatest degree of identity between the two species occurs within the triple-helical domain and the C-terminal non-collagenous domain, whereas the identity within the N-terminal non-collagenous domain is markedly lower. The inter-chain disulphide-bonding observed previously within the triple helix of bovine type X collagen is explained by the presence of two cysteine residues within an imperfection of the triple-helical domain encoded by -Gly-Xaa-Cys-Xaa-Yaa-Cys-Xaa-Yaa-Gly-. Southern-blot analyses of bovine genomic DNA demonstrate that the bovine type X collagen gene is likely to have a condensed structure, similar to that of the chick, with at least 1.3 kb of the coding sequence being contained within one exon.
引用
收藏
页码:141 / 148
页数:8
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