NDLI: Characterization of a fibrillar collagen gene in sponges reveals the early evolutionary appearance of two collagen gene families.

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Characterization of a fibrillar collagen gene in sponges reveals the early evolutionary appearance of two collagen gene families.

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Characterization of a fibrillar collagen gene in sponges reveals the early evolutionary appearance of two collagen gene families.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Garrone, R. Exposito, J. Y.
Description	Author Affiliation: Exposito JY ( Institute of Biology and Chemistry of Proteins, Centre National de la Recherche Scientifique, Lyons, France.);
Abstract	We have characterized cDNA and genomic clones coding for a sponge collagen. The partial cDNA has an open reading frame encoding 547 amino acid residues. The conceptual translation product contains a probably incomplete triple-helical domain (307 amino acids) with one Gly-Xaa-Yaa-Zaa imperfection in the otherwise perfect Gly-Xaa-Yaa repeats and a carboxyl propeptide (240 amino acids) that includes 7 cysteine residues. Amino acid sequence comparisons indicate that this sponge collagen is homologous to vertebrate and sea urchin fibrillar collagens. Partial characterization of the corresponding gene reveals an intron-exon organization clearly related to the fibrillar collagen gene family. The exons coding for the triple-helical domain are 54 base pairs (bp) or multiples thereof, except for a 57-bp exon containing the Gly-Xaa-Yaa-Zaa coding sequence and for two unusual exons of 126 and 18 bp, respectively. This latter 18-bp exon marks the end of the triple-helical domain, contrary to the other known fibrillar collagen genes that contain exons coding for the junction between the triple-helical domain and the carboxyl propeptide. Compared to other fibrillar collagen genes, the introns are remarkably small. Hybridization to blotted RNAs established that the gene transcript is 4.9 kilobases. Together with previous results that showed the existence of a nonfibrillar collagen in the same species, these data demonstrate that at least two collagen gene families are represented in the most primitive metazoa.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	17
Volume Number	87
Language	English
Publisher	National Academy of Sciences
Publisher Date	1990-10-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Biological Evolution Collagen Genetics Genes Multigene Family Porifera Amino Acid Sequence Animals Cloning, Molecular DNA Molecular Sequence Data Restriction Mapping Sequence Homology, Nucleic Acid Comparative Study Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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