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Journal of Virology, April 2009, p. 3397-3401, Vol. 83, No. 7
0022-538X/09/$08.00+0 doi:10.1128/JVI.02500-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Department of Virology, Imperial College London, Norfolk Place, London W2 1PG, United Kingdom,1 Institut de Biologie Structurale Jean-Pierre Ebel, UMR 5075, CEA-CNRS-Université Joseph Fourier, 41 rue Jules Horowitz, 38027 Grenoble Cedex 1, France2
Received 5 December 2008/ Accepted 7 January 2009
The Epstein-Barr virus (EBV) protein BZLF1 contains a bZIP DNA binding domain in which C-terminal tail residues fold back against a zipper region that forms a coiled coil and mediates dimerization. Point mutagenesis in the zipper region reveals the importance of individual residues within the 208SSENDRLR215 sequence that is conserved in C/EBP for transactivation and EBV DNA replication. The restoration of BZLF1 DNA replication activity by the complementation of two deleterious mutations (S208E and D236K) indicates that the interaction of the C-terminal tail and the core zipper is required for DNA replication, identifying a functional role for this structural feature unique to BZLF1.
Published ahead of print on 14 January 2009.
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