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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
10
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pubmed:dateCreated |
1993-10-18
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pubmed:abstractText |
N-Myc encodes a nuclear phosphoprotein that contains a basic region (BR), a helix-loop-helix (HLH) and a leucine zipper (Zip). These motifs are hallmarks of certain transcription factors. In pursuit of the question if N-Myc can activate transcription, we have employed an experimental model involving the yeast transcription factor Gal4. We have first generated fusion proteins containing the Gal4 DNA-binding domain joined to portions of N-Myc. Subsequently we have analysed if chimeric proteins can transactivate the transcription of a reporter under the control of Gal4 binding sites. Here we show that the amino terminal portion of N-Myc activates transcription. Activation maps to a domain highly conserved among Myc-proteins and to other non-conserved sequences, suggesting functional redundancy. Previous studies had documented in vitro association of the RB1 protein with N-Myc (Rustig et al., 1991). We here confirm this observation and identify the region encompassing the transactivation domain as responsible for RB1 binding. Analyses of N-Myc transactivation in retinoblastoma cell line WERI lacking a function RB1 protein gave results similar to those with cell lines having an intact RB1 protein, showing that RB1 protein is not required for transactivation by N-Myc. The present findings leave open the question if deregulated expression of N-Myc contributes to tumorigenesis by transcriptional activation of as yet unidentified target genes or by functionally inactivating the protein encoded by the tumor suppressor gene RB1, or by a combination of both.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GAL4 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Luciferases,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-myc,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Retinoblastoma Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0950-9232
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
8
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pubmed:geneSymbol |
RB1
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2833-8
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:8378092-DNA-Binding Proteins,
pubmed-meshheading:8378092-Fungal Proteins,
pubmed-meshheading:8378092-Gene Expression Regulation, Neoplastic,
pubmed-meshheading:8378092-HeLa Cells,
pubmed-meshheading:8378092-Humans,
pubmed-meshheading:8378092-Luciferases,
pubmed-meshheading:8378092-Proto-Oncogene Proteins c-myc,
pubmed-meshheading:8378092-Recombinant Fusion Proteins,
pubmed-meshheading:8378092-Retinoblastoma Protein,
pubmed-meshheading:8378092-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:8378092-Transcription, Genetic,
pubmed-meshheading:8378092-Transcription Factors,
pubmed-meshheading:8378092-Transcriptional Activation,
pubmed-meshheading:8378092-Tumor Cells, Cultured
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pubmed:year |
1993
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pubmed:articleTitle |
Activation of gene transcription by the amino terminus of the N-Myc protein does not require association with the protein encoded by the retinoblastoma suppressor gene RB1.
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pubmed:affiliation |
Department of Classical and Molecular Cytogenetics, German Cancer Research Center, Heidelberg.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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