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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
1999-5-25
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pubmed:abstractText |
Nopp44/46 is a phosphoprotein of the protozoan parasite Trypanosoma brucei that is localized to the nucleolus. Based on the primary sequence, Nopp44/46 appears to be a protein composed of distinct domains. This communication describes the relationship of these domains to the known functional interactions of the molecule and suggests that the amino-terminal region defines a novel homology region that functions in nucleolar targeting. We have previously shown that Nopp44/46 is capable of interacting with nucleic acids and associating with a protein kinase. Using in vitro transcription and translation, we now demonstrate that the nucleic acid binding function maps to the carboxy-terminal domain of the molecule, a region rich in arginine-glycine-glycine motifs. Our experiments reveal that a central region containing a high proportion of acidic residues is required for association with the protein kinase. Analysis of transfectants expressing epitope-tagged Nopp44/46 deletion constructs showed that the amino-terminal 96 amino acids allowed nuclear and nucleolar accumulation of the protein. This region of the molecule shows homology to several recently described nucleolar proteins. Deletion of a 27-amino-acid region within this domain abrogated nucleolar, but not nuclear, localization. These studies show that Nopp44/46 is composed of distinct modules, each of which plays a different role in molecular interactions. We suggest that this protein could facilitate interactions between sets of nucleolar molecules.
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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/NOPP44-46 protein, Trypanosoma...,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
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 |
Sep
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pubmed:issn |
0021-9533
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
111 ( Pt 17)
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2615-23
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:9701560-Amino Acid Sequence,
pubmed-meshheading:9701560-Animals,
pubmed-meshheading:9701560-Biological Transport,
pubmed-meshheading:9701560-Cell Nucleolus,
pubmed-meshheading:9701560-Molecular Sequence Data,
pubmed-meshheading:9701560-Mutagenesis, Site-Directed,
pubmed-meshheading:9701560-Nuclear Proteins,
pubmed-meshheading:9701560-Nucleic Acids,
pubmed-meshheading:9701560-Phosphoproteins,
pubmed-meshheading:9701560-Phosphorylation,
pubmed-meshheading:9701560-Protein Binding,
pubmed-meshheading:9701560-Protein Kinases,
pubmed-meshheading:9701560-Protein Structure, Tertiary,
pubmed-meshheading:9701560-Protozoan Proteins,
pubmed-meshheading:9701560-RNA-Binding Proteins,
pubmed-meshheading:9701560-Trypanosoma brucei brucei
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pubmed:year |
1998
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pubmed:articleTitle |
Distinct domains of a nucleolar protein mediate protein kinase binding, interaction with nucleic acids and nucleolar localization.
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pubmed:affiliation |
Seattle Biomedical Research Institute, Seattle, WA 98109, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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