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The R1 subunit of herpes simplex virus ribonucleotide reductase has chaperone‐like activity similar to Hsp27
Author(s) -
Chabaud Stéphane,
Lambert Herman,
Sasseville A.Marie-Josée,
Lavoie Hugo,
Guilbault Claire,
Massie Bernard,
Landry Jacques,
Langelier Yves
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)00547-7
Subject(s) - ribonucleotide reductase , protein subunit , chaperone (clinical) , virology , herpes simplex virus , chemistry , biology , virus , biochemistry , medicine , gene , pathology
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 α‐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 α‐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.