1990
DOI: 10.1007/bf00569043
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Herpes simplex virus-encoded ribonucleotide reductase: Evidence for the dissociation/ reassociation of the holoenzyme

Abstract: 35S-labeled cells infected with herpes simplex virus type 1 (HSV-1), temperature-sensitive (ts) mutant ts 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. Mixing 35S-labeled RR1 from ts 1222 with unlabeled RR1/RR2 complex from wild type (wt) infected cells resulted in the formation of a complex between 35S-labeled RR1 and unlabeled RR2, indicating that the complex between the R… Show more

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Cited by 12 publications
(12 citation statements)
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“…A nonapeptide corresponding to the C terminus of R2 has been demonstrated to be an effective and specific inhibitor of HSV RR (Dutia et al, 1986;Cohen et al, 1986). This peptide, YAGAVVNDL, represents a site of interaction on R2 with R1 and inhibits enzyme activity by interfering with subunit association (McClements et al, 1988;Paradis et al, 1988;Darling et al, 1990). The nonapeptide can serve as a lead compound for an antiherpesvirus drug; development would be greatly assisted by structural studies of R1-R2 and Rl-peptide interactions.…”
Section: Introductionmentioning
confidence: 99%
“…A nonapeptide corresponding to the C terminus of R2 has been demonstrated to be an effective and specific inhibitor of HSV RR (Dutia et al, 1986;Cohen et al, 1986). This peptide, YAGAVVNDL, represents a site of interaction on R2 with R1 and inhibits enzyme activity by interfering with subunit association (McClements et al, 1988;Paradis et al, 1988;Darling et al, 1990). The nonapeptide can serve as a lead compound for an antiherpesvirus drug; development would be greatly assisted by structural studies of R1-R2 and Rl-peptide interactions.…”
Section: Introductionmentioning
confidence: 99%
“…They associate to form a holoenzyme complex (Frame et al, 1985;Bacchetti et al, 1986;Ingemarson & Lankinen, 1987) which is more stable than the easily dissociated subunits of the cellular reductase (Thelander et al, 1980). The synthetic YAGAVVNDL peptide, which corresponds to the carboxy-terminal nine amino acids of HSV R2, inhibits HSV RR (Dutia et al, 1986;Cohen et al, 1986a) by interfering with RI-R2 subunit interaction (Dutia et al, 1986;Cohen et al, 1986b;McClements et al, 1988;Darling et al, 1990). Thus the domain located at the C terminus of R2 is likely to be essential for subunit association.…”
Section: Introductionmentioning
confidence: 99%
“…Further, because an active holoenzyme can be formed by the intact RR1 and RR2 subunits, each contained in partially purified extracts of ts1222-and tsl207-infected cells respectively Huang et al, 1988), the oligopeptides were also tested in vitro for their effect on the reconstituted activity. The latter approach was followed because a possible RR1 site involved in subunit interaction may be buried deep in the subunit interface once the complex has been formed and thus be inaccessible to the peptides, although recent experiments indicate that this may not be a problem as the two subunits exist in equilibrium between associated and dissociated states (Darling et al, 1990). As shown in Fig.…”
Section: Is the Site Of The Ts1207 Lesion Located At The Interface Bementioning
confidence: 99%