CKII site in Epstein-Barr virus nuclear protein 2 controls binding to hSNF5/Ini1 and is important for growth transformation.
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.
Kwiatkowski
Bogaslaw
B
VA Puget Sound Health Care System, S-111-ONC, 1660 S. Columbian Way, Seattle, WA 98108, USA.
Chen
Szu Yu Jenny
SY
Schubach
William H
WH
D000595:Amino Acid Sequence; D047390:Casein Kinase II; D002868:Chromosomal Proteins, Non-Histone; D004268:DNA-Binding Proteins / Q000378:metabolism*; D019309:Epstein-Barr Virus Nuclear Antigens / Q000737:chemistry* / Q000378:metabolism; D008969:Molecular Sequence Data; D010766:Phosphorylation; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*; D000071796:SMARCB1 Protein; D014157:Transcription Factors; D014764:Viral Proteins
D002868:Chromosomal Proteins, Non-Histone; D004268:DNA-Binding Proteins; C402641:EBNA-2 protein, Human herpesvirus 4; D019309:Epstein-Barr Virus Nuclear Antigens; D000071796:SMARCB1 Protein; C513266:SMARCB1 protein, human; D014157:Transcription Factors; D014764:Viral Proteins; D047390:Casein Kinase II; D017346:Protein Serine-Threonine Kinases