NDLI: A deubiquitinating activity is conserved in the large tegument protein of the herpesviridae.

Content Provider	Semantic Scholar
Author	Schlieker, Christian Korbel, Gregory Alan
Copyright Year	2005
Abstract	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.
File Format	PDF HTM / HTML
Alternate Webpage(s)	http://jvi.asm.org/content/79/24/15582.full.pdf
PubMed reference number	16306630v1
Volume Number	79
Issue Number	24
Journal	Journal of virology
Language	English
Access Restriction	Open
Subject Keyword	Deubiquitination Embedding Epstein-Barr Virus Herpes Simplex Infections Herpesviridae Homologous Gene Human herpesvirus 1 Largest Murid herpesvirus 1
Content Type	Text
Resource Type	Article

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