The complete intron/exon structure of Ephydatia mülleri fibrillar collagen gene suggests a mechanism for the evolution of an ancestral gene module.
We have completed the analysis of a genomic clone, G238, that contains most of the coding region of the sponge COLF1 fibrillar collagen gene. The main triple helical domain is encoded by 31 exons. Except for the 5' junction exon and the two last 3' exons (126 and 18 base pairs), all these exons are related to a 54-bp unit and begin with an intact glycine codon. A good correlation can be made between this sponge gene and a vertebrate fibrillar collagen gene, revealing the high conservation of the members of this family during evolution. The reconstitution of an ancestral collagen gene can be made by considering all the exon/intron junctions of these genes. We suggest that such an ancestral gene arose from multiple duplications of a 54-bp exon and a (54 + 45)-bp module.
Exposito
J Y
JY
Institut de Biologie et Chimie des Protéines, CNRS UPR 412, Université Claude Bernard, Lyon, France.
van der Rest
M
M
Garrone
R
R
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D005075:Biological Evolution; D003094:Collagen / Q000737:chemistry / Q000235:genetics*; D005091:Exons; D005796:Genes; D007438:Introns; D008957:Models, Genetic; D008969:Molecular Sequence Data; D005810:Multigene Family; D011161:Porifera / Q000235:genetics*; D017433:Protein Structure, Secondary; D012617:Sea Urchins / Q000235:genetics; D014714:Vertebrates / Q000235:genetics
D003094:Collagen