Alpha 1 type IV collagen gene evolved differently from fibrillar collagen genes.
Type IV collagen is a major structural component in basement membranes. It is considerably different from the fibrillar collagens, types I-III. For example, unlike fibrillar collagens, the triple helical domain of type IV collagen is frequently interrupted by nonhelical regions. In this report, we demonstrate several overlapping genomic clones which cover most of the mouse alpha 1(IV) chain. Electron microscopic analysis of R-loops revealed that there were at least 28 exons within 35 kilobases of the gene segment. The sizes of six exons were determined by DNA sequence analysis to be 81, 178, 134, 73, 129, and 213 base pairs. These sizes do not appear to be related to the 54-base pair coding unit which is characteristic of fibrillar collagen exons, suggesting that the alpha 1 type IV collagen gene evolved differently from the fibrillar collagen genes.
D008841:Actin Cytoskeleton / Q000648:ultrastructure; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001485:Basement Membrane / Q000378:metabolism; D005075:Biological Evolution; D002460:Cell Line; D003001:Cloning, Molecular; D003094:Collagen / Q000235:genetics*; D004247:DNA / Q000032:analysis; D004262:DNA Restriction Enzymes; D005796:Genes; D051379:Mice; D009690:Nucleic Acid Conformation; D009693:Nucleic Acid Hybridization; D011487:Protein Conformation; D012333:RNA, Messenger / Q000235:genetics; D013724:Teratoma
D012333:RNA, Messenger; D003094:Collagen; D004247:DNA; D004262:DNA Restriction Enzymes