Open AccessCKII Site in Epstein-Barr Virus Nuclear Protein 2 Controls Binding to hSNF5/Ini1 and Is Important for Growth Transformation
Author(s) -
Bogaslaw Kwiatkowski,
Szu Yu Jenny Chen,
William H. Schubach
Publication year - 2004
Publication title -
journal of virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.617
H-Index - 292
eISSN - 1070-6321
pISSN - 0022-538X
DOI - 10.1128/jvi.78.11.6067-6072.2004
Subject(s) - biology , mutagenesis , transformation (genetics) , binding site , mutation , phosphorylation , alanine , virus , microbiology and biotechnology , virology , genetics , gene , amino acid
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.