The non-structural protein Nsp10 of mouse hepatitis virus binds zinc ions and nucleic acids

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• 作者：Nele Matthes ; Jeroen R. Mesters ; Bruno Coutard ; Bruno Canard ; Eric J. Snijder ; Ralf Moll and Rolf Hilgenfeld
• 关键词：Non-structural protein ; Nsp10 ; Mouse hepatitis virus ; Zinc finger ; RNA/DNA binding protein ; Zone-interference gel electrophoresis
• 刊名：FEBS Letters
• 出版年：2006
• 出版时间：24 July 2006
• 年：2006
• 卷：580
• 期：17
• 页码：4143-4149
• 全文大小：559 K

文摘

The non-structural protein Nsp10 of coronaviruses is a small cleavage product of the viral replicase polyprotein that has been implicated in RNA synthesis. Nsp10 of mouse hepatitis virus (MHV) displays an apparent molecular mass of 13–16 kDa in reducing SDS–PAGE and analytical gel filtration, while dynamic light scattering suggests the existence of oligomeric forms. Atomic absorption spectroscopy reveals two metal ions per Nsp10 monomer, with a preference for Zn²⁺ over Fe^2+/3+ and Co²⁺. These are probably bound by two Zn-finger-like motifs. Moreover, MHV Nsp10 interacts with tRNA, single-stranded RNA, double-stranded DNA and, to a lesser extent, single-stranded DNA as shown by gel-shift experiments. The K_d for tRNA is 2.1 ± 0.2 μM.