Abstract
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 language | English |
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Pages (from-to) | 851-857 |
Number of pages | 7 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 328 |
Issue number | 4 |
DOIs | |
State | Published - 25 Mar 2005 |
Keywords
- Cdk1
- Cdk4
- Cell cycle
- Chromatin immunoprecipitation
- Cyclin B1
- Cyclin D1
- Cyclin E1
- Cyclin H
- Origin of DNA replication
- Purα
- Purγ
- c-MYC gene
- p21