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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
7
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pubmed:dateCreated |
1991-7-11
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pubmed:abstractText |
The Epstein-Barr virus nuclear antigen 2A (EBNA-2A) was immunoprecipitated from latently Epstein-Barr virus-infected lymphocytes with a polyclonal serum raised against the EBNA-2A C terminus. The nucleus contained three subfractions of EBNA-2A which could be distinguished by their resistance to salt extraction: (i) a nucleoplasmatic fraction that was solubilized at 50 mM NaCl, (ii) a chromatin-associated fraction extractable at 1.5 M NaCl, and (iii) a nuclear matrix-associated fraction solubilized only by boiling with buffer containing 2% sodium dodecyl sulfate. The three subfractions were phosphorylated; it was demonstrated that the nucleoplasmatic and the chromatin-associated fractions were phosphorylated at serine and threonine residues. The half-life of the EBNA-2A protein was determined by cycloheximide treatment and by pulse-chase experiments and was found to be at least 24 h. The turnover of the phosphate residues bound to the two salt-soluble subfractions was determined to be approximately 6 to 9 h, suggesting a possible role of the phosphorylation in the regulation of the biological activity of EBNA-2A. Dephosphorylation of EBNA-2A resulted in an increased mobility of the protein during sodium dodecyl sulfate-polyacrylamide gel electrophoresis and indicated the presence of differentially phosphorylated subclasses of the protein. Analysis of EBNA-2A by sucrose gradient centrifugation revealed the existence of two subclasses of complexed molecules which exhibited sedimentation coefficients of approximately 13S and 34S.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1645792-14304234,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1645792-211256,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1645792-211267,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1645792-2153641,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1645792-2154588,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1645792-2157887,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/1645792-2535719,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1645792-2536113,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/1645792-6329907
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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 |
Jul
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pubmed:issn |
0022-538X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
65
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3779-88
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:1645792-Antigens, Viral,
pubmed-meshheading:1645792-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:1645792-Epstein-Barr Virus Nuclear Antigens,
pubmed-meshheading:1645792-Herpesvirus 4, Human,
pubmed-meshheading:1645792-Macromolecular Substances,
pubmed-meshheading:1645792-Molecular Structure,
pubmed-meshheading:1645792-Molecular Weight,
pubmed-meshheading:1645792-Phosphoproteins,
pubmed-meshheading:1645792-Precipitin Tests
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pubmed:year |
1991
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pubmed:articleTitle |
Biochemical characterization of Epstein-Barr virus nuclear antigen 2A.
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pubmed:affiliation |
Abteilung Virologie, Universitätskliniken des Saarlandes, Homburg, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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