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https://doi.org/10.1016/S0014-5793(97)01365-3
Title: | Genomic structure of a potassium channel toxin from Heteractis magnifica | Authors: | Gendeh, G.S. Chung, M.C.M. Jeyaseelan, K. |
Keywords: | Heteractis magnifica Potassium channel toxin |
Issue Date: | 1997 | Citation: | Gendeh, G.S., Chung, M.C.M., Jeyaseelan, K. (1997). Genomic structure of a potassium channel toxin from Heteractis magnifica. FEBS Letters 418 (1-2) : 183-188. ScholarBank@NUS Repository. https://doi.org/10.1016/S0014-5793(97)01365-3 | Abstract: | We provide information on the gene encoding the K+ channel toxin, HmK, of the sea anemone Heteractis magnifica. A series of DNA amplifications by PCR, which included the amplification of the 5'-untranslated region of the gene, showed that an intron of 402 nucleotides separated the sequence that encodes the matured toxin from the signal peptide sequence. A second 264 nucleotide intron interrupted the 5'-untranslated region of the previously reported HmK cDNA. Two possible transcription-initiation sites were identified by primer extension analysis. Corresponding TATA-box consensus sequences, characteristic of a promoter region, were also located from PCR products of uncloned libraries of adaptor-ligated genomic DNA fragments. The coding region for matured HmK is intronless. The same is also true for other sea anemone toxins reported thus far. More notably, a similar intron-exon organization is present in other ion channel-blocking toxins from scorpions implying that molecules having similar functions share a similar organization at the genomic level suggesting a common path of evolution. | Source Title: | FEBS Letters | URI: | http://scholarbank.nus.edu.sg/handle/10635/38253 | ISSN: | 00145793 | DOI: | 10.1016/S0014-5793(97)01365-3 |
Appears in Collections: | Staff Publications |
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