Organization of the exons coding for pro alpha 1(II) collagen N-propeptide confirms a distinct evolutionary history of this domain of the fibrillar collagen genes.
The organization of the exons coding for the N-terminal portion of human type II procollagen has been determined. Aside from inferring the previously unknown primary structure of type II N-propeptide, this study has revealed that this coding domain of the gene exhibits an organization uniquely distinct from those of type I and type III collagens. This finding substantiates the notion that the N-propeptide coding domains of the fibrillar collagen genes evolved under less stringent selection than those encoding the C-propeptide and triple helical regions.
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Department of Microbiology and Immunology, Morse Institute of Molecular Genetics, State University of New York Health Science Center, Brooklyn 11203.
Benson-Chanda
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Vissing
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Ramirez
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F
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D005075:Biological Evolution; D002417:Cattle / Q000235:genetics; D003094:Collagen / Q000235:genetics; D005091:Exons; D005796:Genes; D006801:Humans; D008969:Molecular Sequence Data; D011347:Procollagen / Q000235:genetics*; D012689:Sequence Homology, Nucleic Acid; D013045:Species Specificity
D011347:Procollagen; D003094:Collagen