Unusual Gene Organization in the Protozoan ParasiteEntamoeba histolytica
Autor: | Egbert Tannich, C. Lioutas, Matthias Leippe, Iris Bruchhaus |
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Rok vydání: | 1993 |
Předmět: |
Gene Organization
Genes Protozoan Molecular Sequence Data Protozoan Proteins Ion Channels Superoxide dismutase Entamoeba histolytica fluids and secretions Lectins parasitic diseases Genetics Animals Coding region Molecular Biology Cell Nucleus Membrane Glycoproteins Base Sequence biology Superoxide Dismutase Membrane Proteins Cell Biology General Medicine DNA Protozoan biology.organism_classification Protozoan parasite digestive system diseases Protein Biosynthesis biology.protein |
Zdroj: | DNA and Cell Biology. 12:925-933 |
ISSN: | 1557-7430 1044-5498 |
DOI: | 10.1089/dna.1993.12.925 |
Popis: | 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. |
Databáze: | OpenAIRE |
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