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Virus Genes

, Volume 3, Issue 4, pp 367–372 | Cite as

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

  • Allan J. Darling
  • Elizabeth M. McKay
  • Rolf Ingemarson
  • Brian Booth
Article

Abstract

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.

Key words

HSV ribonucleotide reductase subunit dissociation reassociation 

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Copyright information

© Kluwer Academic Publishers 1990

Authors and Affiliations

  • Allan J. Darling
    • 1
  • Elizabeth M. McKay
    • 1
  • Rolf Ingemarson
    • 2
  • Brian Booth
    • 3
  1. 1.M.R.C. Virology UnitInstitute of VirologyGlasgowScotland
  2. 2.Department of Physiological ChemistryUniversity of UmeaUmeaSweden
  3. 3.Glaxo Group Research Ltd.GreenfordEngland

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