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J Virol, March 1998, p. 2259-2264, Vol. 72, No. 3
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

The Gene Product of Human Cytomegalovirus Open Reading Frame UL56 Binds the pac Motif and Has Specific Nuclease Activity

Elke Bogner,1,2,* Klaus Radsak,2 and Mark F. Stinski1

Department of Microbiology, College of Medicine, University of Iowa, Iowa City, Iowa 52242,1 and Institute of Virology, 35037 Marburg, Germany2

Received 8 September 1997/Accepted 4 December 1997

Using the cis-acting human cytomegalovirus (HCMV) packaging elements (pac 1 and pac 2) as DNA probes, specific DNA-protein complexes were detected by electrophoretic mobility shift assay (EMSA) in both HCMV-infected cell nuclear extracts and recombinant baculovirus-infected cell extracts containing the HCMV p130 (pUL56) protein. DNA-binding proteins, which were common in uninfected and infected cell extracts, were also detected. Mutational analysis showed that only the AT-rich core sequences in these cis-acting motifs, 5'-TAAAAA-3' (pac 1) and 5'-TTTTAT-3' (pac 2), were required for specific DNA-protein complex formation. The specificity of the DNA-protein complexes was confirmed by EMSA competition. Furthermore, a specific endonuclease activity was found to be associated with lysates of baculovirus-infected cells expressing recombinant p130 (rp130). This nuclease activity was time dependent, related to the amount of rp130 in the assay, and ATP independent. Nuclease activity remained associated with rp130 after partial purification by sucrose gradient centrifugation, suggesting that this activity is a property of HCMV p130. We propose a possible involvement of p130 in HCMV DNA packaging.

* Corresponding author. Mailing address: Institute of Virology, Robert-Koch-Str. 17, 35037 Marburg, Germany. Phone: 49-6421-285362. Fax: 49-6421-285482. E-mail: bogner{at}Mailer.Uni-Marburg.De.




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