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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1989 Jan;86(2):592–596. doi: 10.1073/pnas.86.2.592

Structure of the rat argininosuccinate lyase gene: close similarity to chicken delta-crystallin genes.

T Matsubasa 1, M Takiguchi 1, Y Amaya 1, I Matsuda 1, M Mori 1
PMCID: PMC286518  PMID: 2789519

Abstract

Argininosuccinate lyase (EC 4.3.2.1) is an enzyme of arginine biosynthesis and is also involved in the urea cycle in the liver of ureotelic animals. A comparison of cDNA-derived amino acid sequences revealed that argininosuccinate lyase is highly homologous with chicken delta-crystallin, a major structural protein of the eye lens. The gene for the rat argininosuccinate lyase was cloned and its structure was determined. This gene is a single-copy gene about 14 kilobases long and is split into 16 exons. A comparison with chicken delta-crystallin genes revealed that all introns interrupt the protein-coding regions at homologous positions. This close similarity in structural organization provides strong evidence for the view of Piatigorsky et al. [Piatigorsky, J., O'Brien, W. E., Norman, B. L., Kalmuck, K., Wistow, G., Borras, T., Nickerson, J. M. & Wawrousek, E. F. (1988) Proc. Natl. Acad. Sci. USA 85, 3479-3483] that chicken delta 1- and delta 2-crystallin genes evolved by recruitment and duplication of the preexisting argininosuccinate lyase gene and that delta 2-crystallin is probably the direct homologue argininosuccinate lyase.

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Selected References

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