Rothblum C J, Jackman J, Mikovits J, Shukla R R, Kumar A
Department of Biochemistry and Molecular Biology, George Washington University Medical Center, Washington, D.C. 20037, USA.
J Virol. 1995 Aug;69(8):5156-63. doi: 10.1128/JVI.69.8.5156-5163.1995.
Several lines of evidence suggest that cellular proteins play a role during human immunodeficiency virus type 1 (HIV-1) Tat-mediated trans activation. A recent report from this laboratory has shown that a 140-kDa HeLa nuclear protein (p140) binds specifically to the lower stem region of the Tat response element, TAR RNA. Since HIV-1 trans activation is most efficient in proliferating T cells, we investigated the binding of p140 to TAR RNA in unstimulated and mitogen-activated, G1-phase primary T lymphocytes. TAR RNA/protein-binding activity was low in resting cells but increased significantly within 2 h of activation and remained elevated for at least 48 h. Corresponding increases in p140 protein levels were observed with most but not all donors, suggesting that an additional nuclear factor(s) may be required for efficient binding of this protein to TAR RNA in activated T cells.
多条证据表明,细胞蛋白在人类免疫缺陷病毒1型(HIV-1)Tat介导的反式激活过程中发挥作用。本实验室最近的一份报告显示,一种140 kDa的HeLa细胞核蛋白(p140)特异性结合Tat反应元件TAR RNA的下游茎区。由于HIV-1反式激活在增殖的T细胞中效率最高,我们研究了p140在未刺激的以及有丝分裂原激活的G1期原代T淋巴细胞中与TAR RNA的结合情况。TAR RNA/蛋白结合活性在静止细胞中较低,但在激活后2小时内显著增加,并至少持续升高48小时。在大多数但并非所有供体中都观察到p140蛋白水平相应增加,这表明在激活的T细胞中,该蛋白与TAR RNA的有效结合可能还需要其他核因子。