Phosphorylation of the Epstein-Barr virus nuclear antigen 2.
A major in vivo phosphorylation site of the Epstein-Barr virus nuclear antigen 2 (EBNA-2) was found to be localized at the C-terminus of the protein. In vitro phosphorylation studies using casein kinase 1 (CK-1) and casein kinase 2 (CK-2) revealed that EBNA-2 is a substrate for CK-2, but not for CK-1. The CK-2 specific phosphorylation site was localized in the 140 C-terminal amino acids using a recombinant trpE-C-terminal fusion protein. In a similar experiment, the 58 N-terminal amino acids expressed as a recombinant trpE-fusion protein were not phosphorylated. Phosphorylation of a synthetic peptide corresponding to amino acids 464-476 of EBNA-2 as a substrate led to the incorporation of 0.69 mol phosphate/mol peptide indicating that only one of three potential phosphorylation sites within the peptide was modified. The most likely amino acid residues for phosphorylation by CK-2 are Ser469 and Ser470.
Grässer
F A
FA
Institut für Mikrobiologie und Hygiene, Universitätskliniken des Saarlandes, Hamburg, Germany.
Göttel
S
S
Haiss
P
P
Boldyreff
B
B
Issinger
O G
OG
Mueller-Lantzsch
N
N
D000255:Adenosine Triphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D000956:Antigens, Viral / Q000235:genetics / Q000378:metabolism*; D047388:Casein Kinases; D002460:Cell Line; D019309:Epstein-Barr Virus Nuclear Antigens; D004854:Herpesvirus 4, Human / Q000276:immunology*; D006801:Humans; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000302:isolation & purification; D010455:Peptides / Q000138:chemical synthesis / Q000378:metabolism; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D013379:Substrate Specificity
D000956:Antigens, Viral; D019309:Epstein-Barr Virus Nuclear Antigens; D010446:Peptide Fragments; D010455:Peptides; D011993:Recombinant Fusion Proteins; D000255:Adenosine Triphosphate; D011494:Protein Kinases; D047388:Casein Kinases