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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1991-5-8
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pubmed:databankReference |
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M34256,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M90466,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M90694,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M90695,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M92073,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S78945,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S78946,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S78947,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S78948,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S78949,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S78950
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pubmed:abstractText |
The coding sequence deduced from two overlapping cDNA inserts obtained from a pathogenic strain of Entamoeba histolytica revealed a striking homology (greater than 85%) with elongation factor EF-1 alpha from Saccharomyces cerevisiae and Artemia salina. The deduced amino acid sequence predicted a size of 49 kDa, and antibodies raised against the S. cerevisiae EF-1 alpha cross-reacted with an amoebic protein of similar size (45-47 kDa). Sequence analysis of the cDNA revealed that the 5' untranslated region contained a stretch of 190 nucleotides which was perfectly complementary to a segment of the 3' terminal coding region situated 1015 bases downstream of the methionine initiation codon. Electron microscopy of self-renatured cDNA confirmed the potential of such molecules to form a stem-loop secondary structure. The presence of the complementary sequences was confirmed at the genomic level by sequence analysis of polymerase chain reaction-amplified segments which span both the 3' and 5' terminal complementary regions. Comparison of the deduced amino acid sequence of E. histolytica EF-1 alpha with Ef-Tu from Escherichia coli and EF-1 alpha from different sources, suggested that the major functional domains of the protein are located within the loop structure.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0166-6851
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
44
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
23-32
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:2011152-Amino Acid Sequence,
pubmed-meshheading:2011152-Animals,
pubmed-meshheading:2011152-Artemia,
pubmed-meshheading:2011152-Base Sequence,
pubmed-meshheading:2011152-Cloning, Molecular,
pubmed-meshheading:2011152-DNA,
pubmed-meshheading:2011152-DNA, Protozoan,
pubmed-meshheading:2011152-Entamoeba histolytica,
pubmed-meshheading:2011152-Molecular Sequence Data,
pubmed-meshheading:2011152-Nucleic Acid Conformation,
pubmed-meshheading:2011152-Peptide Elongation Factor 1,
pubmed-meshheading:2011152-Peptide Elongation Factors,
pubmed-meshheading:2011152-Saccharomyces cerevisiae,
pubmed-meshheading:2011152-Sequence Homology, Nucleic Acid
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pubmed:year |
1991
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pubmed:articleTitle |
Cloning and characterization of an unusual elongation factor-1 alpha cDNA from Entamoeba histolytica.
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pubmed:affiliation |
MacArthur Center for Molecular Biology of Parasitic Diseases, Weizmann Institute of Science, Rehovot, Israel.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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