Herpes simplex virus-encoded ribonucleotide reductase: evidence for the dissociation/reassociation of the holoenzyme.
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 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 the large subunit of HSV-1 RR and the small subunit of HSV-2.
Darling
A J
AJ
M.R.C. Virology Unit, Institute of Virology, Glasgow, Scotland.
McKay
E M
EM
Ingemarson
R
R
Booth
B
B
D000595:Amino Acid Sequence; D002478:Cells, Cultured; D008969:Molecular Sequence Data; D009154:Mutation; D011233:Precipitin Tests; D012264:Ribonucleotide Reductases / Q000235:genetics* / Q000378:metabolism; D018139:Simplexvirus / Q000201:enzymology / Q000235:genetics*; D013696:Temperature
D012264:Ribonucleotide Reductases