Journal of biosciences | |
Cloning and sequencing of complete ðœ-crystallin cDNA from embryonic lens of Crocodylus palustris | |
Yogendra Sharma1  Anurag Kumar Mishra1  Reena Chandrashekhar1  Ramesh K Aggarwal11  Jetty Ramadevi1  Raman Agrawal1  | |
[1] Centre for Cellular and Molecular Biology, Uppal Road, Hyderabad 500 007, India$$ | |
关键词: ð›¼-enolase; crocodile; gene sharing; lens; ðœ-crystallin; | |
DOI : | |
来源: Indian Academy of Sciences | |
【 摘 要 】
ðœ-Crystallin is a taxon-specific structural protein found in eye lenses. We present here the cloning and sequencing of complete ðœ-crystallin cDNA from the embryonic lens of Crocodylus palustris and establish it to be identical to the ð›¼-enolase gene from non-lenticular tissues. Quantitatively, the ðœ-crystallin was found to be the least abundant crystallin of the crocodilian embryonic lenses. Crocodile ðœ-crystallin cDNA was isolated by RT-PCR using primers designed from the only other reported sequence from duck and completed by 5′- and 3′-rapid amplification of cDNA ends (RACE) using crocodile gene specific primers designed in the study. The complete ðœ-crystallin cDNA of crocodile comprises 1305 bp long ORF and 92 and 409 bp long untranslated 5′-and 3′-ends respectively. Further, it was found to be identical to its putative counterpart enzyme ð›¼-enolase, from brain, heart and gonad, suggesting both to be the product of the same gene. The study thus provides the first report on cDNA sequence of ðœ-crystallin from a reptilian species and also re-confirms it to be an example of the phenomenon of gene sharing as was demonstrated earlier in the case of peking duck. Moreover, the gene lineage reconstruction analysis helps our understanding of the evolution of crocodilians and avian species.
【 授权许可】
Unknown
【 预 览 】
Files | Size | Format | View |
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RO201912040494147ZK.pdf | 254KB | download |