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Volume 272, Number 40, Issue of October 3, 1997 pp. 25394-25400
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

The Nucleotidylylation of Herpes Simplex Virus 1 Regulatory Protein 22 by Human Casein Kinase II

(Received for publication, June 25, 1997)

From The Marjorie B. Kovler Viral Oncology Laboratories, The University of Chicago, Chicago, Illinois 60637

The products of the  genes of herpes simplex virus 1, the infected cells proteins (ICP) 0, 4, 22, and 27 perform regulatory functions, are nucleotidylylated, and share the signaling or recognition sequence (RR(A/T)(P/S)R) that correctly predicted the nucleotidylylation of viral proteins encoded by U_L21, U_L31, U_L49, and U_L47 genes expressed later in infection. Extracts from uninfected HeLa cells or casein kinase II purified from sea star nucleotidylylated the ICP22 moiety of a glutathione S-transferase-ICP22 (GST22P) fusion protein with [-³²P]ATP or [2-³H]ATP. We report that: (i) Purified HeLa cell casein kinase II specifically labeled a glutathione S-transferase fusion protein containing the amino-terminal 151 amino acids of ICP22 with [2-³H]ATP. (ii) Nucleotidylylation of GST-ICP22 by purified enzyme exhibited positive cooperativity (Hill coefficient of 2 and a K of 3.7 µM) and a K_m = 37.7 µM for ATP. (iii) Nucleotidylylation was inhibited by heparin, casein, or ATPS but not by ATPS. (iv) Mutation of the signaling sequence from RRAPRR to LKAPEK abolished nucleotidylylation. We conclude that nucleotidylylation of proteins by casein kinase II requires the presence of the signaling or recognition sequence, involves the cleavage of the phosphodiester bond between the  and  phosphate, and need not be preceded by phosphorylation.

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