期刊
FEBS LETTERS
卷 545, 期 2-3, 页码 213-218出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(03)00547-7
关键词
herpes simplex virus; ribonucleotide reductase R1; anti-apoptotic function; alpha-crystallin domain; chaperone activity; 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. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
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