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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
10
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pubmed:dateCreated |
1994-2-8
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pubmed:databankReference | |
pubmed:abstractText |
We have analyzed three independent genomic loci of the protozoan parasite Entamoeba histolytica that contain coding regions for the iron-containing superoxide dismutase, the pore-forming peptide, and the galactose-inhibitable lectin. All of the three structural genes were found to be closely linked unidirectionally to other coding sequences. The intergenic regions did not exceed 1,350 nucleotides. Nuclear run-on data demonstrated that at least the galactose-inhibitable lectin gene is transcribed in a monocistronic fashion. Comparison of the genomic sequences described here with several others reported previously for E. histolytica revealed a number of invariable peculiarities for the gene organization of this parasite: (i) Coding sequences are not interrupted by introns; (ii) 5' untranslated regions are rather short and transcription starts at the consensus sequences ATTCA or ATCA; (iii) an unusual TATA-motif is located about 30 nucleotides upstream of the start of transcription and comprises the sequence TATTTAAA, which reveals protein binding activity as determined by gel retardation assays; (iv) the conserved pentanucleotide motif TAA/TTT is found within the relatively short 3' untranslated regions and functions putatively as the transcription termination signal; and (v) a stretch of up to 12 pyrmidine residues is located at the end of transcribed sequences.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Protozoan,
http://linkedlifedata.com/resource/pubmed/chemical/Ion Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protozoan Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Superoxide Dismutase,
http://linkedlifedata.com/resource/pubmed/chemical/amoebapore proteins, protozoan,
http://linkedlifedata.com/resource/pubmed/chemical/galactose inhibitable adherence...
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
1044-5498
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
12
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pubmed:geneSymbol |
cEh-FeSOD
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
925-33
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8274224-Animals,
pubmed-meshheading:8274224-Base Sequence,
pubmed-meshheading:8274224-Cell Nucleus,
pubmed-meshheading:8274224-DNA, Protozoan,
pubmed-meshheading:8274224-Entamoeba histolytica,
pubmed-meshheading:8274224-Genes, Protozoan,
pubmed-meshheading:8274224-Ion Channels,
pubmed-meshheading:8274224-Lectins,
pubmed-meshheading:8274224-Membrane Glycoproteins,
pubmed-meshheading:8274224-Membrane Proteins,
pubmed-meshheading:8274224-Molecular Sequence Data,
pubmed-meshheading:8274224-Protein Biosynthesis,
pubmed-meshheading:8274224-Protozoan Proteins,
pubmed-meshheading:8274224-Superoxide Dismutase
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pubmed:year |
1993
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pubmed:articleTitle |
Unusual gene organization in the protozoan parasite Entamoeba histolytica.
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pubmed:affiliation |
Bernhard Nocht Institute for Tropical Medicine, Hamburg, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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