Sumoylation of Rta of Epstein-Barr virus is preferentially enhanced by PIASxβ

Shih Tung Liu, Wen Hung Wang, Yi Ren Hong, Jian Ying Chuang, Pei Jung Lu, Li Kwan Chang

研究成果: 雜誌貢獻文章同行評審

22 引文 斯高帕斯(Scopus)

摘要

Epstein-Barr virus (EBV) expresses an immediate-early protein, Rta, to activate the viral lytic cycle. This study identifies PIASxα and PIASxβ as binding partners of Rta in a yeast two-hybrid screen and demonstrates the binding of Rta to PIASxα and PIASxβ in vitro by GST pull-down analysis. Coimmunoprecipitation experiments and indirect immunofluorescence analysis show that Rta interacts and colocalizes with PIASxα and PIASxβ in the nucleus. These interactions seem to enhance Rta sumoylation as transfecting plasmids expressing PIASxα, PIASxβ, Ubc9, or SUMO-1 increase the capacity of Rta to transactivate a promoter that contains an Rta-response element and the promoters of p21 and BNLF1 in transient transfection assay. This study also finds that Rta sumoylation is preferentially enhanced by PIASxβ, which could be attributed to the fact that PIASxβ, compared to PIASxα, has a strong affinity to Rta, suggesting that affinity of a SUMO E3 ligase to its target protein influences the function of protein sumoylation.
原文英語
頁(從 - 到)163-170
頁數8
期刊Virus Research
119
發行號2
DOIs
出版狀態已發佈 - 八月 2006
對外發佈

ASJC Scopus subject areas

  • 癌症研究
  • 病毒學
  • 傳染性疾病

指紋

深入研究「Sumoylation of Rta of Epstein-Barr virus is preferentially enhanced by PIASxβ」主題。共同形成了獨特的指紋。

引用此