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Herpes simplex virus-encoded ribonucleotide reductase: Evidence for the dissociation/ reassociation of the holoenzyme

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35S-labeled cells infected with herpes simplex virus type 1 (HSV-1), temperature-sensitive (ts) mutantts 1222 were used as a source of the large subunit of the viral ribonucleotide reductase (RR) to investigate the binding of the large (RR1) and small (RR2) subunits in the active enzyme. Mixing35S-labeled RR1 fromts 1222 with unlabeled RR1/RR2 complex from wild type (wt) infected cells resulted in the formation of a complex between35S-labeled RR1 and unlabeled RR2, indicating that the complex between the RR1 and RR2 subunits is dynamic and subunit dissociation/reassociation occurs during enzyme function. Similar results were obtained when unlabeled HSV-2 RR was substituted for HSV-1 RR, demonstrating that the holoenzyme can be formed from the large subunit of HSV-1 RR and the small subunit of HSV-2.

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Requests for reprints should be addressed to Allan J. Darling, The Beatson Institute for Cancer Research, Wolfson Laboratory for Molecular Pathology, Garscube Estate, Switchback Road, Bearsden, Glasgow, G61 1BD, Scotland.

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Darling, A.J., McKay, E.M., Ingemarson, R. et al. Herpes simplex virus-encoded ribonucleotide reductase: Evidence for the dissociation/ reassociation of the holoenzyme. Virus Genes 3, 367–372 (1990). https://doi.org/10.1007/BF00569043

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Key words

  • HSV
  • ribonucleotide reductase
  • subunit dissociation
  • reassociation