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Structure and Assembly | Spotlight

A Deubiquitinating Activity Is Conserved in the Large Tegument Protein of the Herpesviridae

Christian Schlieker, Gregory A. Korbel, Lisa M. Kattenhorn, Hidde L. Ploegh
Christian Schlieker
Department of Pathology, Harvard Medical School, 77 Avenue Louis Pasteur, NRB, Boston, Massachusetts 02115
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Gregory A. Korbel
Department of Pathology, Harvard Medical School, 77 Avenue Louis Pasteur, NRB, Boston, Massachusetts 02115
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Lisa M. Kattenhorn
Department of Pathology, Harvard Medical School, 77 Avenue Louis Pasteur, NRB, Boston, Massachusetts 02115
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Hidde L. Ploegh
Department of Pathology, Harvard Medical School, 77 Avenue Louis Pasteur, NRB, Boston, Massachusetts 02115
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  • For correspondence: ploegh@wi.mit.edu
DOI: 10.1128/JVI.79.24.15582-15585.2005
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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.

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A Deubiquitinating Activity Is Conserved in the Large Tegument Protein of the Herpesviridae
Christian Schlieker, Gregory A. Korbel, Lisa M. Kattenhorn, Hidde L. Ploegh
Journal of Virology Nov 2005, 79 (24) 15582-15585; DOI: 10.1128/JVI.79.24.15582-15585.2005

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A Deubiquitinating Activity Is Conserved in the Large Tegument Protein of the Herpesviridae
Christian Schlieker, Gregory A. Korbel, Lisa M. Kattenhorn, Hidde L. Ploegh
Journal of Virology Nov 2005, 79 (24) 15582-15585; DOI: 10.1128/JVI.79.24.15582-15585.2005
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KEYWORDS

Herpesviridae
Ubiquitins
Viral Proteins

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