Peptides containing cyclin/Cdk-nuclear localization signal motifs derived from viral initiator proteins bind to DNA when unphosphorylated.

Abstract:

: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.

journal_name

J Virol

journal_title

Journal of virology

authors

Kim RJ,Moine S,Reese DK,Bullock PA

doi

10.1128/jvi.76.23.11785-11792.2002

subject

Has Abstract

pub_date

2002-12-01 00:00:00

pages

11785-92

issue

23

eissn

0022-538X

issn

1098-5514

journal_volume

76

pub_type

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