@article{mbs:/content/journal/jgv/10.1099/0022-1317-76-10-2423, author = "Szekely, Laszlo and Jiang, Wei-Qin and Pokrovskaja, Katja and Wiman, Klas G. and Klein, George and Ringertz, Nils", title = "Reversible nucleolar translocation of Epstein—Barr virus-encoded EBNA-5 and hsp70 proteins after exposure to heat shock or cell density congestion", journal= "Journal of General Virology", year = "1995", volume = "76", number = "10", pages = "2423-2432", doi = "https://doi.org/10.1099/0022-1317-76-10-2423", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-76-10-2423", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", abstract = "The Epstein—Barr virus (EBV)-encoded, nuclear matrix-associated EBNA-5 protein is preferentially localized within distinct nuclear blobs in EBV-immortalized lymphoblastoid cell lines. We have previously found that the same blobs also contain retinoblastoma (Rb) protein. We now show that they contain hsp70 protein as well. Both EBNA-5 and hsp70 translocate to the nucleolus under cell density congestion or after heat shock. Both proteins relocate to their original position upon the reestablishment of normal physiological conditions. EBNA-5 is tightly bound to the nuclear matrix. The translocated EBNA-5 is also tightly associated with matrix structures, as shown by sequential elution-based cell fractionation. The Rb protein does not translocate to the nucleolus. The virally encoded EBNA-1, -2, -3 and -6, and cellular PCNA, snRNP and cyclin E are not affected either. The translocation of EBNA-5 to the nucleolus is not species- or cell type-specific since stress conditions induced the same phenomenon in EBNA-5-transfected human, mouse and rat cells of different tissue origins.", }