Functional interaction of Puralpha with the Cdk2 moiety of cyclin A/Cdk2.
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.
Mesh Terms:
Animals, Binding Sites, CDC2-CDC28 Kinases, Cyclin A, Cyclin-Dependent Kinase 2, DNA, DNA-Binding Proteins, Hela Cells, Histones, Humans, Mice, NIH 3T3 Cells, Nerve Tissue Proteins, Phosphorylation, Protein Binding
Animals, Binding Sites, CDC2-CDC28 Kinases, Cyclin A, Cyclin-Dependent Kinase 2, DNA, DNA-Binding Proteins, Hela Cells, Histones, Humans, Mice, NIH 3T3 Cells, Nerve Tissue Proteins, Phosphorylation, Protein Binding
Biochem. Biophys. Res. Commun.
Date: Mar. 25, 2005
PubMed ID: 15707957
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