PMID: 2504933Jul 1, 1989Paper

The border residues of the dihydrofolate reductase domain in Escherichia coli beta-galactosidase correspond to the positions of introns 1 and 5 of dihydrofolate reductase of chicken

Journal of Molecular Evolution
W Kuchinke

Abstract

In beta-galactosidase of Escherichia coli residues 820-934 are similar to residues in dihydrofolate reductase of E. coli. Dihydrofolate reductase of E. coli and chicken are also similar and have identical tertiary structures. I used the similarity of the three-dimensional structure of prokaryotic and eukaryotic dihydrofolate reductases to align the chicken dihydrofolate reductase and the similar residues of beta-galactosidase. The positions of introns 1 and 5 of the chicken dihydrofolate reductase gene correspond exactly to the start and the end of the dihydrofolate reductase-like domain in the beta-galactosidase polypeptide chain. This equivalence of intron positions in a eukaryotic gene and domain structure in a prokaryotic protein was interpreted as evidence for a common origin of both genes.

References

Apr 1, 1977·Proceedings of the National Academy of Sciences of the United States of America·A V Fowler, I Zabin
Jan 1, 1978·Proceedings of the National Academy of Sciences of the United States of America·J M HoodI Zabin
Feb 9, 1978·Nature·W Gilbert
Jul 18, 1986·Cell·W GilbertG McKnight
Feb 1, 1974·Proceedings of the Society for Experimental Biology and Medicine·M KlockarsJ Furth
Apr 17, 1980·Nature·L E Orgel, F H Crick

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