CKII site in Epstein-Barr virus nuclear protein 2 controls binding to hSNF5/Ini1 and is important for growth transformation

J Virol. 2004 Jun;78(11):6067-72. doi: 10.1128/JVI.78.11.6067-6072.2004.

Abstract

Substitution mutagenesis of EBNA2 shows that its interaction with hSNF5/Ini1 involves two sites (286IPP and DQQ313), and a mutation at a CKII phosphorylation site (SS469) is essential for the interaction. An alanine substitution (SS469AA) prevents binding to EBNA2 and diminishes the growth-promotion potential of EBNA2 in the transcomplementation assay.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Casein Kinase II
  • Chromosomal Proteins, Non-Histone
  • DNA-Binding Proteins / metabolism*
  • Epstein-Barr Virus Nuclear Antigens / chemistry*
  • Epstein-Barr Virus Nuclear Antigens / metabolism
  • Molecular Sequence Data
  • Phosphorylation
  • Protein Serine-Threonine Kinases / metabolism*
  • SMARCB1 Protein
  • Transcription Factors
  • Viral Proteins

Substances

  • Chromosomal Proteins, Non-Histone
  • DNA-Binding Proteins
  • EBNA-2 protein, Human herpesvirus 4
  • Epstein-Barr Virus Nuclear Antigens
  • SMARCB1 Protein
  • SMARCB1 protein, human
  • Transcription Factors
  • Viral Proteins
  • Casein Kinase II
  • Protein Serine-Threonine Kinases