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

Nele Matthes, Jeroen R. Mesters, Bruno Coutard, Bruno Canard, Eric J. Snijder, Ralf Moll, Rolf Hilgenfeld*

*Corresponding author for this work
20 Citations (Scopus)

Abstract

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 Fe2+/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 Kd for tRNA is 2.1 ± 0.2 μM.

Original languageEnglish
JournalFEBS Letters
Volume580
Issue number17
Pages (from-to)4143-4149
Number of pages7
ISSN0014-5793
DOIs
Publication statusPublished - 24.07.2006

Research Areas and Centers

  • Academic Focus: Center for Infection and Inflammation Research (ZIEL)

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