Please use this identifier to cite or link to this item: 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
Source: 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
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