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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
26
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pubmed:dateCreated |
1996-8-20
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pubmed:databankReference | |
pubmed:abstractText |
We have previously identified a set of tyrosine-phosphorylated proteins with apparent molecular masses of 44-46 kDa as some of the major tyrosine phosphorylated species in the protozoan parasite Trypanosoma brucei. We now show that these molecules, herein named Nopp44/46, are localized in the nucleolus. Using monoclonal antibodies, we have isolated Nopp44/46 cDNA clones from expression libraries. Sequence analysis reveals that the predicted amino acid sequence of the molecule is composed of an N-terminal unique region, an internal acidic region, and C-terminal repeat region. Analysis of the cDNA clones and genomic Southern analysis indicated that Nopp44/46 belongs to a multigene family in which different gene copies are very similar but vary in the number of repeats. Interestingly, the repetitive amino acid sequence motif contains multiple RGG (Arg-Gly-Gly) boxes characteristic of RNA-binding proteins. In vitro binding experiments demonstrated that Nopp44/46 is indeed capable of binding nucleic acids. Competition experiments with different RNA homopolymers demonstrated that Nopp44/46 preferentially binds to poly(U). These studies suggest that Nopp44/46 may play a role in RNA metabolism in trypanosomes and raise the possibility that tyrosine phosphorylation may regulate the process.
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pubmed:grant | |
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, Single-Stranded,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphotyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/Protozoan Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
28
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pubmed:volume |
271
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
15675-81
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8663171-Amino Acid Sequence,
pubmed-meshheading:8663171-Animals,
pubmed-meshheading:8663171-Base Sequence,
pubmed-meshheading:8663171-Cell Nucleolus,
pubmed-meshheading:8663171-Cloning, Molecular,
pubmed-meshheading:8663171-DNA, Single-Stranded,
pubmed-meshheading:8663171-Genes, Protozoan,
pubmed-meshheading:8663171-Immunohistochemistry,
pubmed-meshheading:8663171-Molecular Sequence Data,
pubmed-meshheading:8663171-Nuclear Proteins,
pubmed-meshheading:8663171-Phosphoproteins,
pubmed-meshheading:8663171-Phosphotyrosine,
pubmed-meshheading:8663171-Protozoan Proteins,
pubmed-meshheading:8663171-RNA-Binding Proteins,
pubmed-meshheading:8663171-Restriction Mapping,
pubmed-meshheading:8663171-Trypanosoma brucei brucei
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pubmed:year |
1996
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pubmed:articleTitle |
A major tyrosine-phosphorylated protein of Trypanosoma brucei is a nucleolar RNA-binding protein.
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pubmed:affiliation |
Seattle Biomedical Research Institute, Seattle, Washington 98109, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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