ArticleJournal of molecular evolution1990
Evolution of collagen IV genes from a 54-base pair exon: a role for introns in gene evolution.
Article in Journal of molecular evolution, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 30 citations in OpenAlex.
- Three reasons protein disorder analysis makes more sense in the light of collagen.Protein science : a publication of the Protein Society · 2016Article
- Collagen XV: exploring its structure and role within the tumor microenvironment.Molecular cancer research : MCR · 2013Review
- Circular permutation directs orthogonal assembly in complex collagen peptide mixtures.The Journal of biological chemistry · 2013Article
- Retrocopy contributions to the evolution of the human genome.BMC genomics · 2008Article
- Determination of the genomic structure of the COL4A4 gene and of novel mutations causing autosomal recessive Alport syndrome.American journal of human genetics · 1998Article
- Evidence for intron capture: an unusual path for the evolution of proteins.Proceedings of the National Academy of Sciences of the United States of America · 1994Article
- The complete intron/exon structure of Ephydatia mülleri fibrillar collagen gene suggests a mechanism for the evolution of an ancestral gene module.Journal of molecular evolution · 1993Article
- Identification of a novel sequence element in the common promoter region of human collagen type IV genes, involved in the regulation of divergent transcription.The Biochemical journal · 1993Article
- Statistical analysis and prediction of the exonic structure of human genes.Journal of molecular evolution · 1992Article
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5 authors at 1 institution in 1 country.
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Abstract
The exon structure of the collagen IV gene provides a striking example for collagen evolution and the role of introns in gene evolution. Collagen IV, a major component of basement membranes, differs from the fibrillar collagens in that it contains numerous interruptions in the triple helical Gly-X-Y repeat domain. We have characterized all 47 exons in the mouse alpha 2(IV) collagen gene and find two 36-, two 45-, and one 54-bp exons as well as one 99- and three 108-bp exons encoding the Gly-X-Y repeat sequence. All these exons sizes are also found in the fibrillar collagen genes. Strikingly, of the 24 interruption sequences present in the alpha 2-chain of mouse collagen IV, 11 are encoded at the exon/intron borders of the gene, part of one interruption sequence is encoded by an exon of its own, and the remaining interruptions are encoded within the body of exons. In such "fusion exons" the Gly-X-Y encoding domain is also derived from 36-, 45-, or 54-bp sequence elements. These data support the idea that collagen IV genes evolved from a primordial 54-bp coding unit. We furthermore interpret these data to suggest that the interruption sequences in collagen IV may have evolved from introns, presumably by inactivation of splice site signals, following which intronic sequences could have been recruited into exons. We speculated that this mechanism could provide a role for introns in gene evolution in general.
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