NDLI: Siah-1b is a direct transcriptional target of p53: Identification of the functional p53 responsive element in the siah-1b promoter

Content Provider	PubMed Central
Author	Fiucci, Giusy Beaucourt, Séverine Dominique, Duflaut Alexandra, Lespagnol Pamela, Stumptner-cuvelette Anne, Géant Buchwalter, Gilles Marcel, Tuynder Susini, Laurent Lassalle, Jean-michel Wasylyk, Christine Wasylyk, Bohdan Oren, Moshe Amson, Robert Telerman, Adam
Copyright Year	2004
Abstract	Siah proteins are E3 ubiquitin ligases. They are homologues of the Drosophila seven in absentia (Sina), a protein required for the R7 photoreceptor development. We have previously found that the expression of human siah-1 and its mouse homologue siah-1b are induced by p53 during apoptosis and tumor reversion. So far, no evidence that the siah-1b gene is a direct transcriptional target of p53 has been provided. In the present study we investigate this issue. Northern blot analysis with a specific probe demonstrates an increase in siah-1b transcription on activation of endogenous and inducible exogenous p53. To explore whether this effect is directly mediated by p53 we analyzed 20 kb of chromosome X DNA, containing the siah-1b locus. A p53-binding site was identified in the siah-1b promoter, located at nucleotides -2155/-2103 relative to the translational start site. This site is composed of two half-sites, conforming to the p53-binding consensus sequence but separated by a nonclassical 33-bp spacer. In luciferase assays, p53 induces a substantial increase in siah-1b promoter activity. Gel shift and DNase-I-footprinting studies, combined with mutational analysis and chromatin immunoprecipitation, indicate that p53 effectively binds the siah-1b promoter in vitro and in vivo. Thus, the siah-1b gene is a direct transcriptional target of p53.
Related Links	http://dx.doi.org/10.1073/pnas.0400177101
Starting Page	3510
File Format	PDF
ISSN	10916490
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	10
Volume Number	101
Language	English
Publisher	National Academy of Sciences
Publisher Date	2004-03-09
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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