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

Authors: Matsubasa, T  Takiguchi, M  Amaya, Y  Matsuda, I  Mori, M 
Citation: Matsubasa T, etal., Proc Natl Acad Sci U S A 1989 Jan;86(2):592-6.
Pubmed: (View Article at PubMed) PMID:2789519

Argininosuccinate lyase (EC 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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RGD Object Information
RGD ID: 632221
Created: 2003-08-28
Species: All species
Last Modified: 2004-05-25
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.