Enhancement of transactivation activity of Rta of Epstein-Barr virus by RanBPM

JOURNAL OF MOLECULAR BIOLOGY

卷:379

Article

Chang, Li-Kwan^1,2  Liu, Shih-Tung³  Kuo, Chung-Wen³  Wang, Wen-Hung³  Chuang, Jian-Ying³  Bianchi, Elisabetta⁴  Hong, Yi-Ren⁵ 

[1] Natl Taiwan Univ, Inst Microbiol & Biochem, Taipei 10617, Taiwan

[2] Natl Taiwan Univ, Dept Biochem Sci & Technol, Taipei 10617, Taiwan

[3] Chang Gung Univ, Mol Genet Lab, Dept Microbiol & Immunol, Tao Yuan 333, Taiwan

[4] Inst Pasteur, Dept Immunol, Immunoregulat Lab, F-75724 Paris, France

[5] Kaohsiung Med Univ, Grad Inst Biochem, Kaohsiung 807, Taiwan

关键词: Epstein-Barr virus;    Rta;    RanBPM;   

DOI  :  10.1016/j.jmb.2008.04.011

来源: Elsevier

【 摘 要 】

Epstein-Barr virus (EBV) expresses the immediate-early protein Rta to activate the transcription of EBV lytic genes and the lytic cycle. We show that RanBPM acts as a binding partner of Rta in yeast two-hybrid analysis. The binding was confirmed by glutathione-S-transferase pull-down assay. A coimmunoprecipitation experiment and confocal microscopy revealed that RanBPM and Rta interact in vivo and colocalize in the nucleus. The interaction appears to involve the SPRY domain in RanBPM and the region between amino acid residues 416 to 476 in Rta. The interaction promotes the transactivation activity of Rta in activating the transcription of BMLF1 and p21 in transient transfection assays. Additionally, RanBPM interacts with SUMO-E2 (Ubc9) to promote sumoylation of Rta by SUMO-1. This fact explains why the expression of RanBPM enhances the transactivation activity of Rta. Taken together, the present results indicate a new role of RanBPM in regulating a viral protein that is critical to EBV lytic activation. (C) 2008 Elsevier Ltd. All rights reserved.

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