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Evolution of aspartyl proteases by gene duplication: the mouse renin gene is organized in two homologous clusters of four exons.
Author(s) -
Holm I.,
Ollo R.,
Panthier J.J.,
Rougeon F.
Publication year - 1984
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1984.tb01846.x
Subject(s) - biology , exon , gene duplication , tandem exon duplication , genetics , gene , intron , genomic dna , restriction enzyme , gene cluster , gene conversion , microbiology and biotechnology , genome
Overlapping recombinant clones that appear to encompass the entire renin gene, named Ren 1, have been isolated from a library of BALB/c mouse genomic DNA fragments. Based on restriction endonuclease mapping and DNA sequence analysis, Ren 1 spans 9.6 kb and contains nine exons interrupted by eight intervening sequences of highly variable size. The first exon, encoding the signal peptide of preprorenin, is separated from the eight following exons by a 3‐kb intron. These eight exons are organized into two clusters of four separated by a 2‐kb intron. DNA stretches encoding the aspartyl residues, which are part of the active site of renin, are located at homologous positions in both clusters. Our results show that aspartyl protease genes have arisen by duplication and fusion of an ancestral gene containing five exons. The estimated date of the duplication event of the mouse renin genes Ren 1 and Ren 2 is discussed.