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Extensive structural differences between genes for the α 1 and α 2 chains of type IV collagen despite conservation of coding sequences
Author(s) -
Hostikka Sirkka Liisa,
Tryggvason Karl
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80473-8
Subject(s) - exon , gene , intron , coding region , genetics , biology , homology (biology) , exon trapping , gene prediction , untranslated region , alternative splicing , genome , rna
Analysis of the structure of the 3′‐end of the human α 2 (IV) gene demonstrated that the α 1 (IV) and α 2 (IV) genes have diverged extensively in spite of the apparent homology of the respective gene products. The NC‐1 domain and the 3′‐untranslated region are encoded by three exons in the α 2 (IV) gene but five exons in the α 1 (IV) gene. The two introns present in the NC‐ 1 domain coding part of the α 2 (IV) gene had the same location as two of the introns of the α 1 (IV) gene. The junction exon in the α 2 (IV) gene contains 53 bp coding for Gly‐X‐Y sequences whereas there are 71 bp in the α 1 (IV) gene. Three other Gly‐X‐Y coding exons studied from the human ⇌ 2 (IV) gene have sizes that differ from corresponding exons in the α 1 (IV) gene and only one intron location matches here between the two genes. None of the exons studied has 54 bp or multiples thereof.