Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow Print PDF (170K) Freely available
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (10)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Remacle, S.
Right arrow Articles by Rezsöhazy, R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Remacle, S.
Right arrow Articles by Rezsöhazy, R.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 2002, Vol. 30, No. 12 2663-2668
© 2002 Oxford University Press

Changing homeodomain residues 2 and 3 of Hoxa1 alters its activity in a cell-type and enhancer dependent manner

Sophie Remacle, Chloë Shaw-Jackson, Christelle Matis, Xavier Lampe, Jacques Picard and René Rezsöhazy*

Unité de Génétique du Développement, UCL 7382, Université Catholique de Louvain, B-1200 Bruxelles, Belgium

The second and third amino acid residues of the N-terminal arm of most Hox protein homeodomains are basic (lysine or arginine), whereas they are asparagine and alanine, respectively, in the Hoxa1 homeodomain. Previous reports pinpointed these residues as specificity determinants in the function of Hoxa1 when it is acting as a monomer. However, in vitro data supported that these residues do not influence the target specificity of Hoxa1 in Pbx1a–Hoxa1 heterodimers. Here, we have analysed the transcriptional activity of a Hoxa1(NA-KR) mutant for which the asparagine and alanine residues of the homeodomain have been replaced by lysine and arginine, respectively. Comparison between the wild-type and mutant Hoxa1 reveals that they show distinct activity on the TSEII enhancer of the somatostatin gene, but that they are equally active in the presence of Pbx and Prep cofactors. This therefore corroborates the biochemical evidence having shown that the second and third residues of the homeodomain do not contribute to the DNA binding of Hoxa1–Pbx dimers. However, on the hoxb1 autoregulatory enhancer, Hoxa1 and Hoxa1(NA-KR) may display distinct activity despite the presence of Pbx, in a cell-type dependent manner. Therefore, our data suggest that, depending on the enhancer, these residues may contribute to the functional specificity of Hoxa1 and that this contribution may not be abrogated by the interaction with Pbx.

* To whom correspondence should be addressed. Tel: +32 2 764 7383; Fax: +32 2 764 7385; Email: rene.rezsohazy{at}gede.ucl.ac.be


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
Y. Liu, K. S. Matthews, and S. E. Bondos
Multiple Intrinsically Disordered Sequences Alter DNA Binding by the Homeodomain of the Drosophila Hox Protein Ultrabithorax
J. Biol. Chem., July 25, 2008; 283(30): 20874 - 20887.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
X. Lampe, O. A. Samad, A. Guiguen, C. Matis, S. Remacle, J. J. Picard, F. M. Rijli, and R. Rezsohazy
An ultraconserved Hox-Pbx responsive element resides in the coding sequence of Hoxa2 and is active in rhombomere 4
Nucleic Acids Res., June 1, 2008; 36(10): 3214 - 3225.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. ProteomicsHome page
S. E. Bondos, X.-X. Tan, and K. S. Matthews
Physical and Genetic Interactions Link Hox Function with Diverse Transcription Factors and Cell Signaling Proteins
Mol. Cell. Proteomics, May 1, 2006; 5(5): 824 - 834.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
S. Remacle, L. Abbas, O. De Backer, N. Pacico, A. Gavalas, F. Gofflot, J. J. Picard, and R. Rezsohazy
Loss of Function but No Gain of Function Caused by Amino Acid Substitutions in the Hexapeptide of Hoxa1 In Vivo
Mol. Cell. Biol., October 1, 2004; 24(19): 8567 - 8575.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.