Functional interaction of Purα with the Cdk2 moiety of cyclin A/Cdk2

Hong Liu, Sharon M. Barr, Caryn Chu, D. Stave Kohtz, Yayoi Kinoshita, Edward M. Johnson

Research output: Contribution to journalArticlepeer-review

25 Scopus citations


Purα is a sequence-specific single-stranded nucleic acid-binding protein and a member of the highly conserved Pur family. Purα has been shown to colocalize with cyclin A/Cdk2 and to coimmunoprecipitate with cyclin A during S-phase. Here we show that this interaction is mediated by a specific affinity of Purα for Cdk2. In pull-down assays GST-Purα efficiently binds Cdk2 and Cdk1, binds Cdk4 less efficiently, and does not display binding to Cdk6. Purα stimulates several-fold the phosphorylation in vitro of histone H1 by cyclin A/Cdk2, produced from baculovirus constructs. Double chromatin immunoprecipitation using antibodies to Cdk2 and Purα reveals that both proteins colocalize in HeLa cells to DNA segments upstream of the c-MYC gene. Pur family member Purγ colocalizes with Cdk2 to a specific DNA segment in this region.

Original languageEnglish
Pages (from-to)851-857
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number4
StatePublished - 25 Mar 2005


  • Cdk1
  • Cdk4
  • Cell cycle
  • Chromatin immunoprecipitation
  • Cyclin B1
  • Cyclin D1
  • Cyclin E1
  • Cyclin H
  • Origin of DNA replication
  • Purα
  • Purγ
  • c-MYC gene
  • p21


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