| Autor: |
Graeme Wistow, J. F. Hejtmancik, John M. Nickerson, Joram Piatigorsky, Toshimichi Shinohara, G Inana, Barbara Norman, J W Hawkins, Teresa Borrás, Charles R. King |
| Rok vydání: |
2008 |
| Předmět: |
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| Zdroj: |
Ciba Foundation Symposium 106-Human Cataract Formation |
| Popis: |
Analysis of recombinant DNAs provides new information on the basis of crystallin evolution and diversity. All crystallin genes contain introns. Two similar, tandemly linked chicken delta-crystallin genes, which probably arose by gene duplication, contain at least 16-17 introns. In the beta-crystallins three introns are situated between exons encoding the structural motifs of the protein, thus relating gene and protein structure. The structurally similar beta- and gamma-crystallins are coded by separate gene families which apparently arose by successive duplications of a common ancestral gene. The N-termini (5' end of gene) of the beta-crystallins appear to have diverged, while the 3' ends have been conserved. In the single murine alpha A-crystallin gene, coding information (the insert exon) for the alpha Ains peptide is contained within an intron. Alternative RNA splicing of this gene gives both the alpha A2 and the alpha Ains crystallin mRNAs. Thus, molecular genetics is providing a deeper appreciation of evolutionary events and is serving to redefine the crystallins in terms of their genes. Since the crystallins are so abundant in the lens, greater understanding of their polypeptide and gene structure should contribute to our understanding of and ability to treat cataract. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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