Journal
JOURNAL OF VIROLOGY
Volume 79, Issue 24, Pages 15582-15585Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.79.24.15582-15585.2005
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Funding
- NIAID NIH HHS [T32 AI007638, T32 AI07638] Funding Source: Medline
- NIGMS NIH HHS [F32 GM072352, GM072352-02] Funding Source: Medline
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The largest tegument protein of herpes simplex virus 1 (HSV-1), UL36, contains a novel deubiquitinating activity embedded in it. All members of the Herpesviridae contain a homologue of HSV-1 UL36, the N-terminal segments of which show perfect conservation of those residues implicated in catalysis. For murine cytomegalovirus and Epstein-Barr virus, chosen as representatives of the beta- and gammaherpesvirus subfamilies, respectively, we here show that the homologous modules indeed display deubiquitinating activity in vitro. The conservation of this activity throughout all subfamilies is indicative of an important, if not essential, function.
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