The non-structural protein Nsp10 of mouse hepatitis virus binds zinc ions and nucleic acids.
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 13-16kDa 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 Zn(2+) over Fe(2+/3+) and Co(2+). 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 microM.
Matthes
Nele
N
Institute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of Lübeck, 23538 Lubeck, Germany.
Mesters
Jeroen R
JR
Coutard
Bruno
B
Canard
Bruno
B
Snijder
Eric J
EJ
Moll
Ralf
R
Hilgenfeld
Rolf
R
D020816:Amino Acid Motifs; D006517:Murine hepatitis virus / Q000737:chemistry* / Q000378:metabolism; D009696:Nucleic Acids / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D017361:Viral Nonstructural Proteins / Q000737:chemistry* / Q000378:metabolism; D015032:Zinc / Q000737:chemistry* / Q000378:metabolism
D009696:Nucleic Acids; D017361:Viral Nonstructural Proteins; D015032:Zinc