A deubiquitinating activity is conserved in the large tegument protein of the herpesviridae.
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.
Schlieker
Christian
C
Department of Pathology, Harvard Medical School, 77 Avenue Louis Pasteur, NRB, Boston, Massachusetts 02115, USA.
Korbel
Gregory A
GA
Kattenhorn
Lisa M
LM
Ploegh
Hidde L
HL
D001665:Binding Sites; D017124:Conserved Sequence; D006564:Herpesviridae / Q000737:chemistry*; D006801:Humans; D014452:Ubiquitins / Q000378:metabolism*; D014764:Viral Proteins / Q000235:genetics / Q000378:metabolism*
C078035:UL36 protein, Human herpesvirus 1; D014452:Ubiquitins; D014764:Viral Proteins