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Journal of Virology, December 2002, p. 11785-11792, Vol. 76, No. 23
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.23.11785-11792.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Peptides Containing Cyclin/Cdk-Nuclear Localization Signal Motifs Derived from Viral Initiator Proteins Bind to DNA When Unphosphorylated

Ronald J. Kim, Stephanie Moine, Danielle K. Reese, and Peter A. Bullock^*

Department of Biochemistry, Tufts University School of Medicine, Boston, Massachusetts 02111

Received 1 July 2002/ Accepted 14 August 2002

A single phosphorylation event at T-antigen residue Thr124 regulates initiation of simian virus 40 DNA replication. To explore this regulatory process, a series of peptides were synthesized, centered on Thr124. These peptides contain a nuclear localization signal (NLS) and a recognition site for cyclin/Cdk kinases. When unphosphorylated, the "CDK/NLS" peptides inhibit T-antigen assembly and bind non-sequence specifically to DNA. However, these activities are greatly reduced upon phosphorylation of Thr124. Similar results were obtained by using peptides derived from the CDK/NLS region of bovine papillomavirus E1. Related studies indicate that residues in the NLS bind to DNA, whereas those in the CDK motif regulate binding. These findings are discussed in terms of the control of T-antigen double hexamer assembly and initiation of viral replication.

Present address: University of Illinois College of Medicine, Urbana-Champaign, IL 61820.

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