| First Author | Liu H | Year | 2005 |
| Journal | Biochem Biophys Res Commun | Volume | 328 |
| Issue | 4 | Pages | 851-7 |
| PubMed ID | 15707957 | Mgi Jnum | J:96495 |
| Mgi Id | MGI:3530718 | Doi | 10.1016/j.bbrc.2005.01.038 |
| Citation | Liu H, et al. (2005) Functional interaction of Puralpha with the Cdk2 moiety of cyclin A/Cdk2. Biochem Biophys Res Commun 328(4):851-7 |
| abstractText | Puralpha is a sequence-specific single-stranded nucleic acid-binding protein and a member of the highly conserved Pur family. Puralpha 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 Puralpha for Cdk2. In pull-down assays GST-Puralpha efficiently binds Cdk2 and Cdk1, binds Cdk4 less efficiently, and does not display binding to Cdk6. Puralpha 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 Puralpha reveals that both proteins colocalize in HeLa cells to DNA segments upstream of the c-MYC gene. Pur family member Purgamma colocalizes with Cdk2 to a specific DNA segment in this region. |
