The R1 subunit of herpes simplex virus ribonucleotide reductase has chaperone-like activity similar to Hsp27.
HSV-2 R1, the R1 subunit of herpes simplex virus (HSV) ribonucleotide reductase, protects cells against apoptosis. Here, we report the presence in HSV-2 R1 of a stretch exhibiting similarity to the alpha-crystallin domain of the small heat shock proteins, a domain known to be important for oligomerization and cytoprotective activities of these proteins. Also, the HSV-2 R1 protein, which forms multimeric structures in the absence of nucleotide, displayed chaperone ability as good as Hsp27 in a thermal denaturation assay using citrate synthase. In contrast, mammalian R1, which does not contain an alpha-crystallin domain, has neither chaperone nor anti-apoptotic activity. Thus, we propose that the chaperone activity of HSV-2 R1 could play an important role in viral pathogenesis.
Chabaud
Stéphane
S
Centre de recherche, Centre hospitalier, Université de Montréal, Montreal, QC, Canada H2L 4M1.
Lambert
Herman
H
Sasseville
A Marie-Josée
AM
Lavoie
Hugo
H
Guilbault
Claire
C
Massie
Bernard
B
Landry
Jacques
J
Langelier
Yves
Y
D000595:Amino Acid Sequence; D017209:Apoptosis; D002950:Citrate (si)-Synthase / Q000378:metabolism; D016384:Consensus Sequence; D006367:HeLa Cells; D006360:Heat-Shock Proteins / Q000378:metabolism*; D018259:Herpesvirus 1, Human / Q000201:enzymology* / Q000235:genetics; D006358:Hot Temperature; D006801:Humans; D007700:Kinetics; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009154:Mutation; D011489:Protein Denaturation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000378:metabolism; D012264:Ribonucleotide Reductases / Q000737:chemistry* / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D014407:Tumor Cells, Cultured
D006360:Heat-Shock Proteins; D011993:Recombinant Fusion Proteins; D012264:Ribonucleotide Reductases; D002950:Citrate (si)-Synthase