Department of Biochemistry, Indian Institute of Science, Bangalore, Karnataka State, India.
FEBS Lett. 2010 Feb 5;584(3):571-6. doi: 10.1016/j.febslet.2009.12.003. Epub 2009 Dec 6.
Open reading frame (ORF) 2a of Sesbania mosaic virus (SeMV) codes for polyprotein 2a (Membrane anchor-protease-VPg-P10-P8). The C-terminal domain of SeMV polyprotein 2a was cloned, expressed and purified in order to functionally characterize it. The protein of size 8kDa (P8) domain, like viral protein genome linked (VPg), was found to be natively unfolded and could bind to nucleic acids. Interestingly, P10-P8 but not P8 showed a novel Mg(2+) dependent ATPase activity that was inhibited in the presence of poly A. In the absence of P8, the ATPase activity of the protein of size 10kDa (P10) domain was reduced suggesting that the natively unfolded P8 domain influenced the P10 ATPase.
开放阅读框（ORF）2a 的芝麻花叶病毒（SeMV）编码多蛋白 2a（膜锚定蛋白酶-VPg-P10-P8）。为了对其进行功能表征，克隆、表达和纯化了 SeMV 多蛋白 2a 的 C 末端结构域。大小为 8kDa（P8）的蛋白域，类似于病毒蛋白基因组连接（VPg），被发现是天然无规卷曲的，能够结合核酸。有趣的是，P10-P8 而非 P8 显示出一种新的 Mg（2+）依赖性 ATP 酶活性，该活性在多聚 A 存在的情况下被抑制。在没有 P8 的情况下，大小为 10kDa（P10）的蛋白域的 ATP 酶活性降低，表明天然无规卷曲的 P8 域影响 P10 ATP 酶。
