대한바이러스학회지 (The Journal of Korean Society of Virology)
- 제28권1호
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- Pages.39-52
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- 1998
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- 1225-2344(pISSN)
p53에 의한 HIV-1 Tat 활성억제와 인산화관련 가능성 연구
p53-mediated Inhibitory Mechanism on HIV-1 Tat is Likely to be Associated with Tat-Phosphorylation
- Byune, Hee-Sun (Hannam University, Department of Microbiology) ;
- Lee, Sang-Gu (Hannam University, Department of Microbiology) ;
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Bae, Yong-Soo
(Hannam University, Department of Microbiology)
- 발행 : 1998.03.30
초록
HIV-1 tat, a strong transactivator, is essential for the HIV-1 replication and AIDS progression. The Tat function is markedly inhibited by human anti-oncogene p53. This work was initiated to identify the p53-associated inhibitory mechanism on tat-mediated transactivation. Inhibitory function of p53 was confirmed by co-transfection of tat-expressing Jurkat cells with LTR-CAT plasmid, or H3T1 cells (LTR-CAT integrated HeLa cells) with different ratio of pSV-tat/pCDNA-p53 plasmids. Results from the direct protein-protein interaction between soluble p53 and tat, and yeast two-hybrid experiments showed that the co-suppression mechanism is unlikely to be due to the direct interaction. CAT activity was not affected by tat in Jurkat cells which were transfected with p53-promoter-CAT or p53-enhancer-CAT, suggesting that the tat-mediated p53 suppression is not directly associated with p53-promoter. Finally, we have tested protein kinase activity in p53-tranfected Jurkat cells, which might phosphorylate HIV-1 tat, resulting in inhibition of tat function. Some of our data lead us to assume that the p53-mediated tat inhibition is likely to be associated with p53-associated, signaling-mediated phosphorylation of tat, resulting in the dysfunction of tat. This study is now under investigation.