PMID- 10597240
OWN - NLM
STAT- MEDLINE
DCOM- 20000110
LR  - 20091119
IS  - 0950-9232 (Print)
IS  - 0950-9232 (Linking)
VI  - 18
IP  - 46
DP  - 1999 Nov 4
TI  - Association of Pur alpha and E2F-1 suppresses transcriptional activity of E2F-1.
PG  - 6398-402
AB  - Protein-protein interaction can play an important role in the control of several 
      biological events including gene transcription, replication and cell
      proliferation. E2F-1 is a DNA-binding transcription factor which, upon
      interaction with its target DNA sequence, induces expression of several S phase
      specific genes allowing progression of the cell cycle. Evidently, the activity of
      this protein is modulated by its cellular partner, pRb, which in the
      hypophosphorylated form, binds to E2F-1 and inactivates its transcriptional
      ability. In this study, we have demonstrated that expression of a
      sequence-specific single-stranded DNA binding protein, Pur alpha, in cells
      decreases the ability of E2F-1 to exert its transcriptional activity upon the
      responsive promoter derived from DHFR. Results from band shift experiments
      revealed that while Pur alpha does not recognize the double-stranded DNA fragment
      containing the E2F-1 binding site, it has the ability to inhibit E2F-1
      interaction with its target DNA sequence. Results from GST pull-down assays and
      the combined immunoprecipitation/Western blot analysis of nuclear extracts
      revealed a direct association of E2F-1 with Pur alpha in the absence of the DNA
      molecule containing the E2F-1 binding site. The association of Pur alpha with
      E2F-1 may increase the stability of E2F-1, as a higher level of E2F-1 was
      detected in cells coexpressing Pur alpha and E2F-1. The importance of these
      observations with respect to the role of Pur alpha in the control of cell cycle
      progression is discussed.
FAU - Darbinian, N
AU  - Darbinian N
AD  - Center for NeuroVirology and NeuroOncology, MCP Hahnemann University School of
      Medicine, Philadelphia, PA 19102, USA.
FAU - Gallia, G L
AU  - Gallia GL
FAU - Kundu, M
AU  - Kundu M
FAU - Shcherbik, N
AU  - Shcherbik N
FAU - Tretiakova, A
AU  - Tretiakova A
FAU - Giordano, A
AU  - Giordano A
FAU - Khalili, K
AU  - Khalili K
LA  - eng
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - England
TA  - Oncogene
JT  - Oncogene
JID - 8711562
RN  - 0 (Carrier Proteins)
RN  - 0 (Cell Cycle Proteins)
RN  - 0 (Cyclic AMP Response Element-Binding Protein)
RN  - 0 (DNA, Single-Stranded)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (E2F Transcription Factors)
RN  - 0 (E2F1 Transcription Factor)
RN  - 0 (E2F1 protein, human)
RN  - 0 (PURA protein, human)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (Retinoblastoma Protein)
RN  - 0 (Retinoblastoma-Binding Protein 1)
RN  - 0 (Transcription Factor DP1)
RN  - 0 (Transcription Factors)
RN  - EC 1.5.1.3 (Tetrahydrofolate Dehydrogenase)
SB  - IM
MH  - Astrocytes
MH  - Binding Sites
MH  - *Carrier Proteins
MH  - Cell Cycle/physiology
MH  - *Cell Cycle Proteins
MH  - Cell Line
MH  - Cell-Free System
MH  - Consensus Sequence
MH  - Cyclic AMP Response Element-Binding Protein/*metabolism
MH  - DNA, Single-Stranded/metabolism
MH  - *DNA-Binding Proteins
MH  - E2F Transcription Factors
MH  - E2F1 Transcription Factor
MH  - Genes, Reporter
MH  - Humans
MH  - Promoter Regions, Genetic
MH  - Protein Binding
MH  - Recombinant Fusion Proteins/biosynthesis
MH  - Retinoblastoma Protein/physiology
MH  - Retinoblastoma-Binding Protein 1
MH  - S Phase
MH  - Tetrahydrofolate Dehydrogenase/genetics
MH  - Transcription Factor DP1
MH  - Transcription Factors/*antagonists & inhibitors/metabolism
MH  - *Transcription, Genetic
MH  - Transfection
EDAT- 1999/12/22 00:00
MHDA- 1999/12/22 00:01
CRDT- 1999/12/22 00:00
PHST- 1999/12/22 00:00 [pubmed]
PHST- 1999/12/22 00:01 [medline]
PHST- 1999/12/22 00:00 [entrez]
AID - 10.1038/sj.onc.1203011 [doi]
PST - ppublish
SO  - Oncogene. 1999 Nov 4;18(46):6398-402. doi: 10.1038/sj.onc.1203011.