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Journal of Virology, December 2007, p. 13659-13667, Vol. 81, No. 24
0022-538X/07/$08.00+0     doi:10.1128/JVI.01204-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Direct Interaction between the N- and C-Terminal Portions of the Herpes Simplex Virus Type 1 Origin Binding Protein UL9 Implies the Formation of a Head-to-Tail Dimer{triangledown}

Soma Chattopadhyay and Sandra K. Weller*

Department of Molecular, Microbial and Structural Biology, University of Connecticut Health Center, Farmington, Connecticut 06030

Received 1 June 2007/ Accepted 3 October 2007

UL9, a superfamily II helicase, is a multifunctional protein required for herpes simplex virus type 1 replication in vivo. Although the C-terminal 317-amino-acid DNA binding domain of UL9 exists as a monomer, the full-length protein behaves as a dimer in solution. Thus, it has been assumed that the N-terminal 534 residues contain a region necessary for efficient dimerization and that UL9 dimers are in a head-to-head configuration. We recently showed, however, that residues in the N terminus could modulate the inhibitory properties of UL9 by decreasing the DNA binding ability of the C terminus (S. Chattopadhyay and S. K. Weller, J. Virol. 80:4491-4500, 2006). We suggested that a direct interaction between the N- and C-terminal portions of UL9 might exist and serve to modulate the DNA binding activities of the C terminus. In this study, we used a coimmunoprecipitation assay to show that the N-terminal portion of UL9 can indeed directly interact with the C terminus. A series of truncation mutant proteins were used to show that a region in the N terminus between residues 293 and 321 is necessary for efficient interaction. Similarly, a region in the C terminus between residues 600 and 800 is required for this interaction. The simplest model to explain these data is that UL9 dimers are oriented in a head-to-tail arrangement in which the N terminus is in contact with the C terminus.

* Corresponding author. Mailing address: Department of Molecular, Microbial, and Structural Biology, MC3205, University of Connecticut Health Center, 263 Farmington Avenue, Farmington, CT 06030. Phone: (860) 679-2310. Fax: (860) 679-1239. E-mail: Weller{at}NSO2.uchc.edu

{triangledown} Published ahead of print on 17 October 2007.

Journal of Virology, December 2007, p. 13659-13667, Vol. 81, No. 24
0022-538X/07/$08.00+0     doi:10.1128/JVI.01204-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.





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