Yang X, Gold M O, Tang D N, Lewis D E, Aguilar-Cordova E, Rice A P, Herrmann C H
Division of Molecular Virology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA.
Proc Natl Acad Sci U S A. 1997 Nov 11;94(23):12331-6. doi: 10.1073/pnas.94.23.12331.
We have previously identified a cellular protein kinase activity termed TAK that specifically associates with the HIV types 1 and 2 Tat proteins. TAK hyperphosphorylates the carboxyl-terminal domain of the large subunit of RNA polymerase II in vitro in a manner believed to activate transcription [Herrmann, C. H. & Rice, A. P. (1995) J. Virol. 69, 1612-1620]. We show here that the catalytic subunit of TAK is a known human kinase previously named PITALRE, which is a member of the cyclin-dependent family of proteins. We also show that TAK activity is elevated upon activation of peripheral blood mononuclear cells and peripheral blood lymphocytes and upon differentiation of U1 and U937 promonocytic cell lines to macrophages. Therefore, in HIV-infected individuals TAK may be induced in T cells following activation and in macrophages following differentiation, thus contributing to high levels of viral transcription and the escape from latency of transcriptionally silent proviruses.
我们之前鉴定出一种细胞蛋白激酶活性，称为TAK，它能特异性地与1型和2型HIV的Tat蛋白结合。TAK在体外能使RNA聚合酶II大亚基的羧基末端结构域发生过度磷酸化，其方式被认为可激活转录[赫尔曼，C. H. & 赖斯，A. P.（1995年）《病毒学杂志》69卷，第1612 - 1620页]。我们在此表明，TAK的催化亚基是一种已知的人类激酶，之前名为PITALRE，它是细胞周期蛋白依赖性蛋白家族的成员。我们还表明，在外周血单核细胞和外周血淋巴细胞被激活时，以及U1和U937原单核细胞系分化为巨噬细胞时，TAK活性会升高。因此，在HIV感染个体中，TAK可能在T细胞激活后以及巨噬细胞分化后被诱导，从而导致高水平的病毒转录以及转录沉默的原病毒从潜伏状态中逃逸。
