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

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.

journal_name

J Virol

journal_title

Journal of virology

authors

Schlieker C,Korbel GA,Kattenhorn LM,Ploegh HL

doi

10.1128/JVI.79.24.15582-15585.2005

subject

Has Abstract

pub_date

2005-12-01 00:00:00

pages

15582-5

issue

24

eissn

0022-538X

issn

1098-5514

pii

79/24/15582

journal_volume

79

pub_type

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