The RING finger domain of Varicella-Zoster virus ORF61p has E3 ubiquitin ligase activity that is essential for efficient autoubiquitination and dispersion of Sp100-containing nuclear bodies. Academic Article uri icon

Overview

MeSH

  • Amino Acid Sequence
  • Amino Acid Substitution
  • Cell Nucleus
  • Immediate-Early Proteins
  • Molecular Sequence Data
  • Protein Stability

MeSH Major

  • Antigens, Nuclear
  • Autoantigens
  • Herpesvirus 3, Human
  • RING Finger Domains
  • Ubiquitin-Protein Ligases
  • Viral Proteins
  • Virus Replication

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 date

  • July 2010

has subject area

  • Amino Acid Sequence
  • Amino Acid Substitution
  • Antigens, Nuclear
  • Autoantigens
  • Cell Nucleus
  • Herpesvirus 3, Human
  • Immediate-Early Proteins
  • Molecular Sequence Data
  • Protein Stability
  • RING Finger Domains
  • Ubiquitin-Protein Ligases
  • Viral Proteins
  • Virus Replication

Research

keywords

  • Journal Article

Identity

Language

  • eng

PubMed Central ID

  • PMC2903287

Digital Object Identifier (DOI)

  • 10.1128/JVI.00335-10

PubMed ID

  • 20392849

Additional Document Info

start page

  • 6861

end page

  • 6865

volume

  • 84

number

  • 13