Document Detail

An alternative model of H ferritin promoter transactivation by c-Jun.
MedLine Citation:
PMID:  11903046     Owner:  NLM     Status:  MEDLINE    
c-Jun is a member of the activator protein 1 family, and its interaction with different nuclear factors generates a wide spectrum of complexes that regulate transcription of different promoters. H ferritin promoter transcription is tightly dependent on nuclear factor Y (NFY). Ferritin transcription is activated by c-Jun, although the promoter does not contain a canonical binding site. NFY, on the other hand, does not bind c-Jun in vitro, whereas in vivo c-Jun is found in the complex containing NFY. Moreover, a c-Jun-GCN4 chimaeric construct containing only the transactivation domain of Jun and the basic-region leucine-zipper domain of GCN4 stimulates the H ferritin promoter. A synthetic GAL4 promoter and the cognate activator, the fusion protein NFY-GAL4, are potently activated by c-Jun. Titration of p300 by co-expressing E1A abolishes the stimulatory effect. Moreover, another p300-dependent promoter, the cAMP-response element, can be superactivated by c-Jun using the same mechanism. These data indicate that c-Jun, when activated or overexpressed, is recruited to the H ferritin promoter by p300, which links NFY, bound to DNA, to the complex. These results add a new level of complexity to transcriptional regulation by c-Jun, which can activate p300-dependent promoters without binding directly to the target DNA.
Maria C Faniello; Giuseppa Chirico; Barbara Quaresima; Giovanni Cuda; Giovanna Allevato; Maria A Bevilacqua; Francesco Baudi; Vittorio Colantuoni; Filiberto Cimino; Salvatore Venuta; Vittorio E Avvedimento; Francesco Costanzo
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The Biochemical journal     Volume:  363     ISSN:  0264-6021     ISO Abbreviation:  Biochem. J.     Publication Date:  2002 Apr 
Date Detail:
Created Date:  2002-03-20     Completed Date:  2002-05-17     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  2984726R     Medline TA:  Biochem J     Country:  England    
Other Details:
Languages:  eng     Pagination:  53-8     Citation Subset:  IM    
Dipartimento di Medicina Sperimentale e Clinica, Università degli Studi di Catanzaro, Via T. Campanella, I-88100 Catanzaro, Italy.
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MeSH Terms
Binding Sites
Blotting, Western
Cell Line
Chloramphenicol O-Acetyltransferase / metabolism
Cyclic AMP / metabolism
Ferritins / genetics*
Hela Cells
Nuclear Proteins / metabolism
Precipitin Tests
Promoter Regions, Genetic*
Protein Binding
Protein Structure, Tertiary
Proto-Oncogene Proteins c-jun / metabolism
Recombinant Fusion Proteins / metabolism
Recombinant Proteins / metabolism
Trans-Activators / metabolism
Transcription, Genetic
Transcriptional Activation*
Reg. No./Substance:
0/Nuclear Proteins; 0/Proto-Oncogene Proteins c-jun; 0/Recombinant Fusion Proteins; 0/Recombinant Proteins; 0/Trans-Activators; 60-92-4/Cyclic AMP; 9007-73-2/Ferritins; EC O-Acetyltransferase

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