| Molecular characterization on the genome structure of hemolysin toxin isoforms isolated from sea anemone Actineria villosa and Phyllodiscus semoni. | |
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MedLine Citation:
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PMID: 20837039 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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We recently identified the existence of new isoforms of Avt-I (from sea anemone Actineria villosa) and Pstx20 (from sea anemone Phyllodiscus semoni) hemolytic toxins, and named them Avt-II and Pst-I. Avt-II and Pst-I differ in length by 14 and 7 bp, respectively, as compared to their corresponding isoform genes. Both newly found isoform genes have the coding regions with the identical length of 1033 bp. The restriction fragment length polymorphism analysis with endonuclease HphI was able to clearly distinguish between the two Avt isoforms, but not Pstx isoforms, and based on the densitometric analysis of DNA bands, it indicated that relative expression levels of Avt-I and Avt-II genes were 18.3% and 81.7%, respectively. PCR amplification of the two Avt isoform genes using the genomic DNA as template indicated the existence of two introns within each toxin isoform gene. The first intron with the identical 242 bp in length for both Avt isoform was found within the 5'-untranslated region, and the second intron with lengths of 654 bp and 661 bp in Avt-I and Avt-II isoforms, respectively, was found within the signal sequence coding region. This is for the first time to identify the existence of introns within hemolysin genes of sea anemone. Having several unique characteristics that have identified only for a new member of actinoporin family of A. villosa and P. semoni, e.g., strong toxicity and genes with introns, it is plausible to speculate that these toxins have a unique genetic evolutionary linage differed from that for other sea anemone hemolytic toxins. |
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Authors:
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Gen-Ichiro Uechi; Hiromu Toma; Takeshi Arakawa; Yoshiya Sato |
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Publication Detail:
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Type: Journal Article Date: 2010-09-15 |
Journal Detail:
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Title: Toxicon : official journal of the International Society on Toxinology Volume: 56 ISSN: 1879-3150 ISO Abbreviation: Toxicon Publication Date: 2010 Dec |
Date Detail:
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Created Date: 2010-11-01 Completed Date: 2011-03-07 Revised Date: 2011-04-25 |
Medline Journal Info:
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Nlm Unique ID: 1307333 Medline TA: Toxicon Country: England |
Other Details:
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Languages: eng Pagination: 1470-6 Citation Subset: IM |
Copyright Information:
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Copyright © 2010. Published by Elsevier Ltd. |
Affiliation:
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Department of Virology, Institute of Tropical Medicine, Nagasaki University, 1-12-4 Sakamoto Nagasaki City, Nagasaki 852 8523, Japan. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Animals Base Sequence Cnidarian Venoms / chemistry*, genetics, isolation & purification Genome* Hemolysin Proteins / chemistry*, genetics, isolation & purification Introns Molecular Sequence Data Phylogeny Polymorphism, Restriction Fragment Length Protein Isoforms / chemistry*, genetics, isolation & purification Sea Anemones / chemistry* Sequence Alignment Sequence Analysis, DNA |
| Chemical | |
Reg. No./Substance:
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0/Cnidarian Venoms; 0/Hemolysin Proteins; 0/Protein Isoforms |
| Comments/Corrections | |
Erratum In:
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Toxicon. 2011 Mar 15;57(4):625 |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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