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...

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Veröffentlicht in:	Biochemical and biophysical research communications 2005-03, Vol.328 (4), p.851-857
Hauptverfasser:	Liu, Hong, Barr, Sharon M, Chu, Caryn, Kohtz, D Stave, Kinoshita, Yayoi, Johnson, Edward M
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Binding Sites CDC2-CDC28 Kinases - chemistry CDC2-CDC28 Kinases - metabolism Cyclin A - chemistry Cyclin A - metabolism Cyclin-Dependent Kinase 2 DNA - chemistry DNA - metabolism DNA-Binding Proteins - chemistry DNA-Binding Proteins - metabolism HeLa Cells Histones - chemistry Histones - metabolism Humans Mice Nerve Tissue Proteins - chemistry Nerve Tissue Proteins - metabolism NIH 3T3 Cells Phosphorylation Protein Binding
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