痘病毒表达的假定枢纽蛋白的生化和生物物理特性。
Biochemical and biophysical properties of a putative hub protein expressed by vaccinia virus.
机构信息
Department of Molecular Genetics and Microbiology, University of Florida, Gainesville, Florida 32610-0266, USA.
出版信息
J Biol Chem. 2013 Apr 19;288(16):11470-81. doi: 10.1074/jbc.M112.442012. Epub 2013 Mar 8.
Abstract
H5 is a constitutively expressed, phosphorylated vaccinia virus protein that has been implicated in viral DNA replication, post-replicative gene expression, and virus assembly. For the purpose of understanding the role of H5 in vaccinia biology, we have characterized its biochemical and biophysical properties. Previously, we have demonstrated that H5 is associated with an endoribonucleolytic activity. In this study, we have shown that this cleavage results in a 3'-OH end suitable for polyadenylation of the nascent transcript, corroborating a role for H5 in vaccinia transcription termination. Furthermore, we have shown that H5 is intrinsically disordered, with an elongated rod-shaped structure that preferentially binds double-stranded nucleic acids in a sequence nonspecific manner. The dynamic phosphorylation status of H5 influences this structure and has implications for the role of H5 in multiple processes during virus replication.
摘要
H5 是一种组成型表达、磷酸化的牛痘病毒蛋白，它与病毒 DNA 复制、复制后基因表达和病毒装配有关。为了了解 H5 在牛痘生物学中的作用，我们对其生化和生物物理特性进行了表征。此前，我们已经证明 H5 与内切核糖核酸酶活性有关。在这项研究中，我们表明这种切割导致 3'-OH 末端适合新生转录物的多聚腺苷酸化，证实了 H5 在牛痘转录终止中的作用。此外，我们还表明 H5 是无规则卷曲的，具有拉长的棒状结构，优先以序列非特异性方式结合双链核酸。H5 的动态磷酸化状态影响这种结构，并对 H5 在病毒复制过程中的多个过程中的作用有影响。
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