爱泼斯坦-巴尔病毒裂解开关蛋白BZLF1多聚化区域天然变体的生物物理分析
Biophysical analysis of natural variants of the multimerization region of Epstein-Barr virus lytic-switch protein BZLF1.
作者信息
Hicks M R, Balesaria S, Medina-Palazon C, Pandya M J, Woolfson D N, Sinclair A J
机构信息
School of Biological Sciences, School of Biological Sciences, University of Sussex, Brighton, East Sussex BN1 9QG, United Kingdom.
出版信息
J Virol. 2001 Jun;75(11):5381-4. doi: 10.1128/JVI.75.11.5381-5384.2001.
Abstract
BZLF1 plays a key role in the induction of Epstein-Barr virus (EBV) replication. On the basis of limited sequence homology and mutagenesis experiments, BZLF1 has been described as a member of the bZip family of transcription factors, but this prospect has not been rigorously tested to date. Here, we present biophysical analysis of the multimerization domain of BZLF1, from three natural variants of EBV, and demonstrate for the first time that the region between amino acids 196 and 227 is sufficient to direct folding as a coiled-coil dimer in vitro.
摘要
BZLF1在爱泼斯坦-巴尔病毒（EBV）复制的诱导过程中起关键作用。基于有限的序列同源性和诱变实验，BZLF1被描述为转录因子bZip家族的成员，但这一推测迄今为止尚未经过严格验证。在此，我们对来自EBV三种天然变体的BZLF1多聚化结构域进行了生物物理分析，并首次证明氨基酸196至227之间的区域足以在体外指导其折叠形成卷曲螺旋二聚体。
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