Genomic structure of a potassium channel toxin from Heteractis magnifica
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 enc...
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Veröffentlicht in: | FEBS letters 1997-11, Vol.418 (1), p.183-188 |
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creator | Gendeh, Gurmil S Chung, Max C.M Jeyaseelan, Kandiah |
description | 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. |
doi_str_mv | 10.1016/S0014-5793(97)01365-3 |
format | Article |
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+ 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.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/S0014-5793(97)01365-3</identifier><identifier>PMID: 9414123</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Amino Acid Sequence ; Animals ; Base Sequence ; Cnidarian Venoms - biosynthesis ; Cnidarian Venoms - chemistry ; Cnidarian Venoms - genetics ; Consensus Sequence ; DNA, Complementary ; Exons ; Genome ; Heteractis magnifica ; Introns ; Molecular Sequence Data ; Polymerase Chain Reaction ; Potassium Channel Blockers ; Potassium channel toxin ; Sea Anemones - genetics ; TATA Box ; Transcription, Genetic</subject><ispartof>FEBS letters, 1997-11, Vol.418 (1), p.183-188</ispartof><rights>1997 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0014-5793(97)01365-3$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9414123$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gendeh, Gurmil S</creatorcontrib><creatorcontrib>Chung, Max C.M</creatorcontrib><creatorcontrib>Jeyaseelan, Kandiah</creatorcontrib><title>Genomic structure of a potassium channel toxin from Heteractis magnifica</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>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.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Cnidarian Venoms - biosynthesis</subject><subject>Cnidarian Venoms - chemistry</subject><subject>Cnidarian Venoms - genetics</subject><subject>Consensus Sequence</subject><subject>DNA, Complementary</subject><subject>Exons</subject><subject>Genome</subject><subject>Heteractis magnifica</subject><subject>Introns</subject><subject>Molecular Sequence Data</subject><subject>Polymerase Chain Reaction</subject><subject>Potassium Channel Blockers</subject><subject>Potassium channel toxin</subject><subject>Sea Anemones - genetics</subject><subject>TATA Box</subject><subject>Transcription, Genetic</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kE9LxDAUxIMo67r6ERZy1EM1r0nT5iSy6K6w4EE9hzR51ci2XZJU9Nvb_YOn4THDY-ZHyBzYLTCQd6-MgciKUvFrVd4w4LLI-AmZQlXyjAtZnZLpf-ScXMT4xca7AjUhEyVAQM6nZLXErm-9pTGFwaYhIO0baui2TyZGP7TUfpquww1N_Y_vaBP6lq4wYTA2-Uhb89H5xltzSc4as4l4ddQZeX96fFussvXL8nnxsM4wl3nKJKu5rZ0SFgpmKyaEc-BqIbgweQ2G20KNHQtsCicEw9I0UgJ35RioDXN8RuaHv9uhbtHpbfCtCb_6uGj07w8-jiW-PQYdrcfOovMBbdKu9xqY3iHUe4R6x0erUu8Ras7_AODnYrc</recordid><startdate>19971124</startdate><enddate>19971124</enddate><creator>Gendeh, Gurmil S</creator><creator>Chung, Max C.M</creator><creator>Jeyaseelan, Kandiah</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope></search><sort><creationdate>19971124</creationdate><title>Genomic structure of a potassium channel toxin from Heteractis magnifica</title><author>Gendeh, Gurmil S ; Chung, Max C.M ; Jeyaseelan, Kandiah</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-e262t-60b3cbd94c150c8044dd1db4434a2b1a3c591815ef5d440e7af6613d7434ba0d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Cnidarian Venoms - biosynthesis</topic><topic>Cnidarian Venoms - chemistry</topic><topic>Cnidarian Venoms - genetics</topic><topic>Consensus Sequence</topic><topic>DNA, Complementary</topic><topic>Exons</topic><topic>Genome</topic><topic>Heteractis magnifica</topic><topic>Introns</topic><topic>Molecular Sequence Data</topic><topic>Polymerase Chain Reaction</topic><topic>Potassium Channel Blockers</topic><topic>Potassium channel toxin</topic><topic>Sea Anemones - genetics</topic><topic>TATA Box</topic><topic>Transcription, Genetic</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gendeh, Gurmil S</creatorcontrib><creatorcontrib>Chung, Max C.M</creatorcontrib><creatorcontrib>Jeyaseelan, Kandiah</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gendeh, Gurmil S</au><au>Chung, Max C.M</au><au>Jeyaseelan, Kandiah</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Genomic structure of a potassium channel toxin from Heteractis magnifica</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1997-11-24</date><risdate>1997</risdate><volume>418</volume><issue>1</issue><spage>183</spage><epage>188</epage><pages>183-188</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><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.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>9414123</pmid><doi>10.1016/S0014-5793(97)01365-3</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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source | MEDLINE; Wiley Free Content; ScienceDirect Journals (5 years ago - present); EZB-FREE-00999 freely available EZB journals; Wiley Online Library All Journals; Alma/SFX Local Collection |
subjects | Amino Acid Sequence Animals Base Sequence Cnidarian Venoms - biosynthesis Cnidarian Venoms - chemistry Cnidarian Venoms - genetics Consensus Sequence DNA, Complementary Exons Genome Heteractis magnifica Introns Molecular Sequence Data Polymerase Chain Reaction Potassium Channel Blockers Potassium channel toxin Sea Anemones - genetics TATA Box Transcription, Genetic |
title | Genomic structure of a potassium channel toxin from Heteractis magnifica |
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