Collagen gene construction and evolution.
Collagen genes appear to have been assembled by the tandem repetition of homologous primary (9 base pair), secondary (54 base pair), and tertiary (702 base pair) modules. In vertebrate interstitial collagen genes many of the secondary modules are separated by introns, but in invertebrate collagen genes the non-coding sequences lie near the ends of supposed tertiary modules and are therefore about 702 (54 X 13) base pairs apart. The genes for vertebrate interstitial collagens (types I-III) seem to have been constructed by the tandem repetition of five tertiary modules, three of which were subsequently shortened by internal deletions. This shortening of the gene resulted in the non-integral relationship between the period of the fibrils and the length of the molecules of vertebrate collagens, and was therefore responsible for the mechanical properties of the completed product. Comparisons of the amino acid sequences of various collagens indicate that the main types of collagen evolved about 800-900 million years ago, a date that agrees well with the fossil record of primitive Metazoa.
D000818:Animals; D001482:Base Composition; D001483:Base Sequence; D005075:Biological Evolution; D002417:Cattle; D002645:Chickens; D003094:Collagen / Q000235:genetics*; D004330:Drosophila / Q000235:genetics; D005580:Fossils; D005796:Genes; D012091:Repetitive Sequences, Nucleic Acid; D012689:Sequence Homology, Nucleic Acid; D013045:Species Specificity
D003094:Collagen