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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1-2
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pubmed:dateCreated |
1989-7-5
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pubmed:abstractText |
A toxic lectin from Phoradendron californicum (PCL) was found to inactivate catalytically 60 S ribosomal subunits of rabbit reticulocytes, resulting in the inhibition of protein synthesis. To study the mechanism of action of PCL, rat liver ribosomes were treated with the toxin and the extracted rRNA was treated with aniline. A fragment containing about 450 nucleotides was released from the 28 S rRNA. Analysis of the nucleotide sequence of the fragment revealed that the aniline-sensitive phosphodiester bond was between A4324 and G4325 of the 28 S rRNA. These results indicate that PCL inactivates the ribosomes by cleaving an N-glycosidic bond at A4324 of 28 S rRNA in the ribosomes as does ricin A-chain.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
8
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pubmed:volume |
248
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
115-8
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:2721668-Animals,
pubmed-meshheading:2721668-Base Sequence,
pubmed-meshheading:2721668-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:2721668-Glycosides,
pubmed-meshheading:2721668-Hydrolysis,
pubmed-meshheading:2721668-Lectins,
pubmed-meshheading:2721668-Liver,
pubmed-meshheading:2721668-N-Glycosyl Hydrolases,
pubmed-meshheading:2721668-Nucleotides,
pubmed-meshheading:2721668-Plant Lectins,
pubmed-meshheading:2721668-Plants, Toxic,
pubmed-meshheading:2721668-Protein Biosynthesis,
pubmed-meshheading:2721668-RNA, Ribosomal, 28S,
pubmed-meshheading:2721668-Rabbits,
pubmed-meshheading:2721668-Rats,
pubmed-meshheading:2721668-Reticulocytes,
pubmed-meshheading:2721668-Ribosome Inactivating Proteins,
pubmed-meshheading:2721668-Ribosomes
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pubmed:year |
1989
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pubmed:articleTitle |
The mechanism of action of the cytotoxic lectin from Phoradendron californicum: the RNA N-glycosidase activity of the protein.
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pubmed:affiliation |
Department of Biochemistry, Yamanashi Medical College, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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