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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
1995-4-14
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pubmed:abstractText |
The cell cycle-dependent transcription factor, E2F-1, regulates the cyclin-like species of the DNA repair enzyme uracil-DNA glycosylase (UDG) gene in human osteosarcoma (Saos-2) cells. We demonstrate, through the deletion of the human UDG promoter sequences, that expression of E2F-1 activates the UDG promoter through several E2F sites. The major putative downstream site for E2F, located in the first exon, serves as a target for E2F-1/DP1 complex binding in vitro. We also provide evidence for the functional relationship between the cyclin-like UDG gene product and E2F. High levels of UDG expression in a transient transfection assay result in the down-regulation of transcriptional activity through elements specific for E2F-mediated transcription. Overexpression of UDG in Saos 2 cells was observed to delay growth late in G1 phase and transiently arrest these cells from progressing into the S phase. This hypothetical model integrates one mechanism of DNA repair with the cell cycle control of gene transcription, likely through E2F. This implicates E2F as a multifunctional target for proteins and enzymes, possibly, responsive to DNA damage through the negative effect of UDG on E2F-mediated transcriptional activity.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD19,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Differentiation...,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Chloramphenicol O-Acetyltransferase,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Glycosylases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/E2F Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/E2F1 Transcription Factor,
http://linkedlifedata.com/resource/pubmed/chemical/E2F1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/N-Glycosyl Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Retinoblastoma-Binding Protein 1,
http://linkedlifedata.com/resource/pubmed/chemical/TFDP1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factor DP1,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Uracil-DNA Glycosidase
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
270
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5289-98
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:7534293-Antigens, CD,
pubmed-meshheading:7534293-Antigens, CD19,
pubmed-meshheading:7534293-Antigens, Differentiation, B-Lymphocyte,
pubmed-meshheading:7534293-B-Lymphocytes,
pubmed-meshheading:7534293-Base Sequence,
pubmed-meshheading:7534293-Bone Neoplasms,
pubmed-meshheading:7534293-Carrier Proteins,
pubmed-meshheading:7534293-Cell Cycle,
pubmed-meshheading:7534293-Cell Cycle Proteins,
pubmed-meshheading:7534293-Cell Division,
pubmed-meshheading:7534293-Cell Line,
pubmed-meshheading:7534293-Chloramphenicol O-Acetyltransferase,
pubmed-meshheading:7534293-DNA Glycosylases,
pubmed-meshheading:7534293-DNA Primers,
pubmed-meshheading:7534293-DNA-Binding Proteins,
pubmed-meshheading:7534293-E2F Transcription Factors,
pubmed-meshheading:7534293-E2F1 Transcription Factor,
pubmed-meshheading:7534293-Flow Cytometry,
pubmed-meshheading:7534293-G1 Phase,
pubmed-meshheading:7534293-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:7534293-Gene Expression Regulation, Neoplastic,
pubmed-meshheading:7534293-Homeostasis,
pubmed-meshheading:7534293-Humans,
pubmed-meshheading:7534293-Molecular Sequence Data,
pubmed-meshheading:7534293-Mutagenesis, Site-Directed,
pubmed-meshheading:7534293-N-Glycosyl Hydrolases,
pubmed-meshheading:7534293-Osteosarcoma,
pubmed-meshheading:7534293-Polymerase Chain Reaction,
pubmed-meshheading:7534293-Promoter Regions, Genetic,
pubmed-meshheading:7534293-Recombinant Proteins,
pubmed-meshheading:7534293-Restriction Mapping,
pubmed-meshheading:7534293-Retinoblastoma-Binding Protein 1,
pubmed-meshheading:7534293-S Phase,
pubmed-meshheading:7534293-Transcription, Genetic,
pubmed-meshheading:7534293-Transcription Factor DP1,
pubmed-meshheading:7534293-Transcription Factors,
pubmed-meshheading:7534293-Transfection,
pubmed-meshheading:7534293-Tumor Cells, Cultured,
pubmed-meshheading:7534293-Uracil-DNA Glycosidase
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pubmed:year |
1995
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pubmed:articleTitle |
E2F-1 and a cyclin-like DNA repair enzyme, uracil-DNA glycosylase, provide evidence for an autoregulatory mechanism for transcription.
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pubmed:affiliation |
Department of Pediatrics, Mount Sinai School of Medicine, New York, New York 10029.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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