Four DNA-dependent ATPases were purified from vaccinia virions and tested for DNA helicase activity on two dsDNA substrates. ATPases D6R and D11L were inactive on both substrates, A18R unwound the substrate with a short 20 bp duplex region and 18R unwound both substrates. In addition, the I8R protein was stimulated to unwind longer DNA duplexes by a 25 kDa protein purified from vaccinia virions, representing the cleaved product of the L4R gene, an ssDNA binding protein. Purified recombinant 25 kDa L4R protein also stimulated I8R DNA helicase activity and maximum activity was observed only when there were < 13 nucleotides of DNA per molecule of L4R protein. The DNA helicase activity of the A18R protein was not stimulated by either recombinant 25 kDa L4R protein or by an ssDNA binding protein.


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