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 α-crystallin domain of the small heat shock proteins, a domain known to be important for oligomerizati...
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| Veröffentlicht in: | FEBS letters 2003-06, Vol.545 (2), p.213-218 |
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| creator | Chabaud, Stéphane Lambert, Herman Sasseville, A.Marie-Josée Lavoie, Hugo Guilbault, Claire Massie, Bernard Landry, Jacques Langelier, Yves |
| description | 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. |
| doi_str_mv | 10.1016/S0014-5793(03)00547-7 |
| format | Article |
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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. 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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.</description><subject>Amino Acid Sequence</subject><subject>Anti-apoptotic function</subject><subject>Apoptosis</subject><subject>Chaperone activity</subject><subject>Citrate (si)-Synthase - metabolism</subject><subject>Consensus Sequence</subject><subject>Heat-Shock Proteins - metabolism</subject><subject>HeLa Cells</subject><subject>Herpes simplex virus</subject><subject>Herpesvirus 1, Human - enzymology</subject><subject>Herpesvirus 1, Human - genetics</subject><subject>Hot Temperature</subject><subject>Hsp27</subject><subject>Humans</subject><subject>Kinetics</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>Mutation</subject><subject>Protein Denaturation</subject><subject>Protein Structure, Secondary</subject><subject>Protein Structure, Tertiary</subject><subject>Recombinant Fusion Proteins - chemistry</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Ribonucleotide reductase R1</subject><subject>Ribonucleotide Reductases - chemistry</subject><subject>Ribonucleotide Reductases - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><subject>Tumor Cells, Cultured</subject><subject>α-Crystallin domain</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkVGL1DAUhYMo7uzoT1DyJO5D9aZJm_RJdNl1hAVB1-eQprdMNNPUpB2df286M-jjCoFwc7-cc7mHkBcM3jBg9duvAEwUlWz4a-BXAJWQhXxEVkxJXnBRq8dk9Re5IJcpfYdcK9Y8JResVCCkVCvi77dIvzCa5nYe3ERDT7cYR0w0ud3o8TfduzgnGl0bhtl6DJPrkEbsZjuZhHRrErVbM2IMAxbe_UBq7OT2bjosEs6bSKdAN2ks5TPypDc-4fPzvSbfbm_urzfF3eePn67f3xW2qpUsVC95y5tSlBYNz7PKXHABtquBG2F40wpb9YCiA2VaZoxgTcP6vBaLsmN8TV6ddMcYfs6YJr1zyaL3ZsAwJy05lyCEehBkDat5JcoMVifQxpBSxF6P0e1MPGgGeslDH_PQy7I15LPkkX3W5OXZYG532P37dQ4gA5sT8Mt5PPyfqr69-VAeO0sD-PF58Xp3ksK82r3DqJN1OFjsXEQ76S64B6b9A4GDrjk</recordid><startdate>20030619</startdate><enddate>20030619</enddate><creator>Chabaud, Stéphane</creator><creator>Lambert, Herman</creator><creator>Sasseville, A.Marie-Josée</creator><creator>Lavoie, Hugo</creator><creator>Guilbault, Claire</creator><creator>Massie, Bernard</creator><creator>Landry, Jacques</creator><creator>Langelier, Yves</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TM</scope><scope>7U9</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>20030619</creationdate><title>The R1 subunit of herpes simplex virus ribonucleotide reductase has chaperone-like activity similar to Hsp27</title><author>Chabaud, Stéphane ; 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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.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>12804778</pmid><doi>10.1016/S0014-5793(03)00547-7</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Anti-apoptotic function Apoptosis Chaperone activity Citrate (si)-Synthase - metabolism Consensus Sequence Heat-Shock Proteins - metabolism HeLa Cells Herpes simplex virus Herpesvirus 1, Human - enzymology Herpesvirus 1, Human - genetics Hot Temperature Hsp27 Humans Kinetics Molecular Sequence Data Molecular Weight Mutation Protein Denaturation Protein Structure, Secondary Protein Structure, Tertiary Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - metabolism Ribonucleotide reductase R1 Ribonucleotide Reductases - chemistry Ribonucleotide Reductases - metabolism Sequence Homology, Amino Acid Tumor Cells, Cultured α-Crystallin domain |
| title | The R1 subunit of herpes simplex virus ribonucleotide reductase has chaperone-like activity similar to Hsp27 |
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