Abstract
Varicella zoster virus encodes an immediate-early (IE) protein termed ORF61p that is orthologous to the herpes simplex virus IE protein ICP0. Although these proteins share several functional properties, ORF61p does not fully substitute for ICP0. The greatest region of similarity between these proteins is a RING finger domain. We demonstrate that disruption of the ORF61p RING finger domain by amino acid substitution (Cys19Gly) alters ORF61p intranuclear distribution and abolishes ORF61p-mediated dispersion of Sp100-containing nuclear bodies. In addition, we demonstrate that an intact ORF61p RING finger domain is necessary for E3 ubiquitin ligase activity and is required for autoubiquitination and regulation of protein stability.
Publication types
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Research Support, N.I.H., Extramural
MeSH terms
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Amino Acid Sequence
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Amino Acid Substitution / genetics
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Antigens, Nuclear / metabolism*
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Autoantigens / metabolism*
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Cell Nucleus / chemistry
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Herpesvirus 3, Human / genetics
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Herpesvirus 3, Human / physiology*
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Immediate-Early Proteins / genetics
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Immediate-Early Proteins / metabolism
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Molecular Sequence Data
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Protein Stability
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RING Finger Domains*
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Ubiquitin-Protein Ligases / genetics
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Ubiquitin-Protein Ligases / metabolism*
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Viral Proteins / genetics
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Viral Proteins / metabolism*
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Virus Replication*
Substances
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Antigens, Nuclear
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Autoantigens
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Immediate-Early Proteins
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Viral Proteins
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protein 61, Varicella-zoster virus
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SP100 protein, human
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Ubiquitin-Protein Ligases
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Vmw110 protein, Human herpesvirus 1