Epstein-Barr virus protein kinase BGLF4 interacts with viral transactivator BZLF1 and regulates its transactivation activity
Epstein-Barr virus protein kinase BGLF4 interacts with viral transactivator BZLF1 and regulates its transactivation activity
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DOI：
10.1099/vir.0.010462-0
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发表时间：
2009-07-01
影响因子：
3.8
通讯作者：
Kawaguchi, Yasushi
中科院分区：
文献类型：
--
作者：
Asai, Risa;Kato, Ai;Kawaguchi, Yasushi
BGLF4是由Epstein-Barr病毒编码的丝氨酸/苏氨酸蛋白激酶。BGLF4的生理底物之一是病毒反式激活因子BZLF1。在本研究中，BZLF1第209位丝氨酸残基(S209A)的丙氨酸替代消除了BGLF4在体外对该蛋白的磷酸化作用。BZLF1的S209A突变和BGLF4的K102I突变也抑制了稳定的BGLF4-BZLF1复合体的形成和BGLF4介导的BZLF1自反式激活活性的下调。这些结果表明，BGLF4-BZLF1形成稳定的复合体能够下调BZLF1的自身调节活性，BZLF1的BGLF4磷酸化可能参与了这一过程。
BGLF4 is a serine/threonine protein kinase encoded by Epstein-Barr virus. One of the physiological substrates of BGLF4 is viral transactivator BZLF1. In the present study, it was demonstrated that alanine substitution of the serine residue at position 209 (S209A) in BZLF1 eliminated phosphorylation of the protein by BGLF4 in vitro. The S209A mutation in BZLF1, as well as a K102I mutation in BGLF4, which inactivated catalytic activity of the viral kinase, also inhibited formation of a stable BGLF4-BZLF1 complex and downregulation of BZLF1 autotransactivation activity mediated by BGLF4. These results indicate that formation of a stable complex of BGLF4-BZLF1 enables downregulation of BZLF1 autoregulation activity and it appears that BGLF4 phosphorylation of BZLF1 may be involved in these processes.