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Functional interaction of Puralpha with the Cdk2 moiety of cyclin A/Cdk2.
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- Author(s): Liu H;Liu H; Barr SM; Chu C; Kohtz DS; Kinoshita Y; Johnson EM
- Source:
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2005 Mar 25; Vol. 328 (4), pp. 851-7.
- Publication Type:
Journal Article; Research Support, U.S. Gov't, P.H.S.
- Language:
English
- Additional Information
- Source:
Publisher: Elsevier Country of Publication: United States NLM ID: 0372516 Publication Model: Print Cited Medium: Print ISSN: 0006-291X (Print) Linking ISSN: 0006291X NLM ISO Abbreviation: Biochem Biophys Res Commun Subsets: MEDLINE
- Publication Information:
Publication: <2002- >: San Diego, CA : Elsevier
Original Publication: New York, Academic Press.
- Subject Terms:
- Abstract:
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.
- Grant Information:
CA55219 United States CA NCI NIH HHS; NS35000 United States NS NINDS NIH HHS
- Accession Number:
0 (Cyclin A)
0 (DNA-Binding Proteins)
0 (Histones)
0 (Nerve Tissue Proteins)
0 (Pura protein, mouse)
9007-49-2 (DNA)
EC 2.7.11.22 (CDC2-CDC28 Kinases)
EC 2.7.11.22 (CDK2 protein, human)
EC 2.7.11.22 (Cdk2 protein, mouse)
EC 2.7.11.22 (Cyclin-Dependent Kinase 2)
- Publication Date:
Date Created: 20050215 Date Completed: 20050408 Latest Revision: 20120625
- Publication Date:
20250114
- Accession Number:
10.1016/j.bbrc.2005.01.038
- Accession Number:
15707957
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