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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
1998-7-6
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pubmed:abstractText |
Human proliferation-associated protein p120 has previously been shown to localize to the nucleolus, and several functional domains of p120 have been elucidated. By using a nitrocellulose filter binding assay and a Northwestern blotting procedure this study shows that recombinant p120 binds to an rRNA fragment in vitro with a dissociation constant of 4 nM. The specific RNA-binding region of p120 (residues 1-57) was identified with glutathione S-transferase-fused p120 deletion constructs and Northwestern blotting procedures. This RNA-binding region of p120, which includes the nucleolar localization signal of p120, is similar to the arginine-rich RNA-binding regions found in other RNA-binding proteins such as HIV Rev and Tat. Experiments in vivo with HeLa cell nucleolar extracts showed that p120 was associated with the 60-80S pre-ribosomal particles. This association is disrupted by treatment with either RNase A or buffer of high ionic strength. These results suggest that p120 might be involved in rRNA/ribosome maturation, consistent with the role of the yeast homologue Nop2p in rRNA biogenesis.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531475-1394192,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531475-1426041,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531475-1457403,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531475-1728415,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531475-1873497,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531475-1907891,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531475-1934059,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531475-2017166,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531475-2256932,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531475-2372471,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531475-2476805,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531475-2477156,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531475-2576976,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531475-2784194,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531475-2914325,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531475-2933102,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531475-3275869,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531475-3422591,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531475-4351171,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531475-4366268,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531475-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531475-6347247,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531475-639809,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531475-679997,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531475-7515880,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531475-7806561,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531475-8036511,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531475-8089149,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531475-8095498,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531475-8344933,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531475-8972218
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Arginine,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/NOP2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Ribosomal,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/tRNA Methyltransferases
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
331 ( Pt 2)
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
387-93
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:9531475-Amino Acid Sequence,
pubmed-meshheading:9531475-Arginine,
pubmed-meshheading:9531475-Binding, Competitive,
pubmed-meshheading:9531475-Binding Sites,
pubmed-meshheading:9531475-Blotting, Northern,
pubmed-meshheading:9531475-Blotting, Western,
pubmed-meshheading:9531475-Cell Nucleolus,
pubmed-meshheading:9531475-Gene Deletion,
pubmed-meshheading:9531475-Glutathione Transferase,
pubmed-meshheading:9531475-HeLa Cells,
pubmed-meshheading:9531475-Humans,
pubmed-meshheading:9531475-Molecular Sequence Data,
pubmed-meshheading:9531475-Mutagenesis, Site-Directed,
pubmed-meshheading:9531475-Nuclear Proteins,
pubmed-meshheading:9531475-Protein Precursors,
pubmed-meshheading:9531475-RNA, Ribosomal,
pubmed-meshheading:9531475-Recombinant Fusion Proteins,
pubmed-meshheading:9531475-Recombinant Proteins,
pubmed-meshheading:9531475-Ribonucleoproteins,
pubmed-meshheading:9531475-tRNA Methyltransferases
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pubmed:year |
1998
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pubmed:articleTitle |
Nucleolar protein p120 contains an arginine-rich domain that binds to ribosomal RNA.
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pubmed:affiliation |
Department of Pharmacology, Baylor College of Medicine, 1 Baylor Plaza, Houston, TX 77030, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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