Article (Scientific journals)
Ikappab-Alpha Enhances Transactivation by the Hoxb7 Homeodomain-Containing Protein
Chariot, Alain; Princen, Frédéric; Gielen, Jacques et al.
1999In Journal of Biological Chemistry, 274 (9), p. 5318-25
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Abstract :
[en] Combinatorial interactions between distinct transcription factors generate specificity in the controlled expression of target genes. In this report, we demonstrated that the HOXB7 homeodomain-containing protein, which plays a key role in development and differentiation, physically interacted in vitro with IkappaB-alpha, an inhibitor of NF-kappaB activity. This interaction was mediated by the IkappaB-alpha ankyrin repeats and C-terminal domain as well as by the HOXB7 N-terminal domain. In transient transfection experiments, IkappaB-alpha markedly increased HOXB7-dependent transcription from a reporter plasmid containing a homeodomain consensus-binding sequence. This report therefore showed a novel function for IkappaB-alpha, namely a positive regulation of transcriptional activation by homeodomain-containing proteins.
Research center :
Giga-Signal Transduction - ULiège
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Chariot, Alain ;  Université de Liège - ULiège > Département de pharmacie > Chimie médicale
Princen, Frédéric
Gielen, Jacques
Merville, Marie-Paule ;  Université de Liège - ULiège > Département de pharmacie > Chimie médicale
Franzoso, Guido
Brown, Keith
Siebenlist, Ulrich
Bours, Vincent ;  Université de Liège - ULiège > Département des sciences biomédicales et précliniques > Génétique générale et humaine
Language :
English
Title :
Ikappab-Alpha Enhances Transactivation by the Hoxb7 Homeodomain-Containing Protein
Publication date :
10 February 1999
Journal title :
Journal of Biological Chemistry
ISSN :
0021-9258
eISSN :
1083-351X
Publisher :
American Society for Biochemistry and Molecular Biology, United States - Maryland
Volume :
274
Issue :
9
Pages :
5318-25
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 11 December 2008

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