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Papers In Press, published online ahead of print June 30, 2004
Microbiology and Immunology, Chang Gung University, Kwei-Shan 333
Corresponding Author: cgliu{at}mail.cgu.edu.tw
Epstein-Barr virus (EBV) expresses an immediate-early protein, Rta, to activate the transcription of EBV lytic genes and the lytic cycle. This work identifies Ubc9 and PIAS1 as binding partners of Rta in a yeast two-hybrid screen. These bindings are verified by GST pull-down assay, coimmunoprecipitation, and confocal microscopy. The interactions appear to cause Rta sumoylation since not only can Rta be sumoylated in vitro but also sumoylated Rta can be detected in P3HR1 cells following lytic induction and in 293T cells after transfecting plasmids that express Rta and SUMO-1. Moreover, PIAS1 stimulates conjugation of SUMO-1 to Rta, thus acting as an E3 ligase. Furthermore, transfecting plasmids that express Ubc9, PIAS1, and SUMO-1, increases the capacity of Rta to transactivate the promoter that includes an Rta-response element, indicating that the modification by SUMO-1 increases the transactivation activity of Rta. This study reveals that Rta is sumoylated at the K19, K213, and K517 residues and that SUMO-1 conjugation at the K19 residue is crucial for enhancing the transactivation activity of Rta. These results indicate that sumoylation of Rta may be important in EBV lytic activation.
J. Biol. Chem, 10.1074/jbc.M405470200
Submitted on May 17, 2004
Revised on June 29, 2004
Accepted on June 30, 2004
Posttranslational modification of Rta of Epstein-Barr virus by SUMO-1
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