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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1998-7-29
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pubmed:databankReference |
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pubmed:abstractText |
Protein p120 is a proliferation-related nucleolar protein which is detectable early in the G1 phase of the cell cycle and peaks early in the S phase. Most human malignant tumors contain much higher levels of protein p120 than normal resting cells. To identify p120-associated protein(s), a yeast two-hybrid screen was carried out using protein p120 as the bait. Two positive clones encoded portions of a novel protein, designated microspherule protein 58 kDa (MSP58). MSP58 mRNA is 1.9 kb and encodes an approximately 58-kDa polypeptide of 462 amino acids as shown by Western blotting of HeLa nucleolar proteins. The mouse MSP58 homolog has 97% amino acid similarity to human MSP58, but no MSP58 homolog was found in the yeast genome. The MSP58 N-terminal region contains serine-rich clusters and its C-terminal region has a coiled-coil domain. In insect Sf9 cells, recombinant p120 and MSP58 proteins associated with each other, confirming the results of the yeast two-hybrid assay. Deletion mutations revealed that the binding of MSP58 to p120 required a previously unrecognized coiled-coil domain within the N-terminal region of p120 and the C-terminal region of MSP58 protein. Immunofluorescence indicated that the MSP58 protein is localized in microspherules in the nucleolus. Anti-MSP58 Ig labeled nucleolar 'caps' when HeLa cells were treated with actinomycin D. When the MSP58 protein was overexpressed in COS-7 cells, the nucleolus became irregularly enlarged, which suggests that MSP58 may affect the size and shape of the nucleolus.
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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/Antigens, Neoplasm,
http://linkedlifedata.com/resource/pubmed/chemical/Chromosomal Proteins, Non-Histone,
http://linkedlifedata.com/resource/pubmed/chemical/Dactinomycin,
http://linkedlifedata.com/resource/pubmed/chemical/NOP2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Nol1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/fibrillarin,
http://linkedlifedata.com/resource/pubmed/chemical/tRNA Methyltransferases
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0014-2956
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
253
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
734-42
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:9654073-Amino Acid Sequence,
pubmed-meshheading:9654073-Animals,
pubmed-meshheading:9654073-Antigens, Neoplasm,
pubmed-meshheading:9654073-Binding Sites,
pubmed-meshheading:9654073-Cell Fractionation,
pubmed-meshheading:9654073-Cell Line,
pubmed-meshheading:9654073-Cell Nucleolus,
pubmed-meshheading:9654073-Cell Nucleus,
pubmed-meshheading:9654073-Chromosomal Proteins, Non-Histone,
pubmed-meshheading:9654073-Cloning, Molecular,
pubmed-meshheading:9654073-Crosses, Genetic,
pubmed-meshheading:9654073-Dactinomycin,
pubmed-meshheading:9654073-HeLa Cells,
pubmed-meshheading:9654073-Humans,
pubmed-meshheading:9654073-Mice,
pubmed-meshheading:9654073-Molecular Sequence Data,
pubmed-meshheading:9654073-Molecular Weight,
pubmed-meshheading:9654073-Nuclear Proteins,
pubmed-meshheading:9654073-RNA-Binding Proteins,
pubmed-meshheading:9654073-Recombinant Proteins,
pubmed-meshheading:9654073-Saccharomyces cerevisiae,
pubmed-meshheading:9654073-Sequence Alignment,
pubmed-meshheading:9654073-Sequence Homology, Amino Acid,
pubmed-meshheading:9654073-Spodoptera,
pubmed-meshheading:9654073-Transfection,
pubmed-meshheading:9654073-tRNA Methyltransferases
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pubmed:year |
1998
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pubmed:articleTitle |
The 58-kDa microspherule protein (MSP58), a nucleolar protein, interacts with nucleolar protein p120.
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pubmed:affiliation |
Department of Pharmacology, Baylor College of Medicine, Houston, TX 77030, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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