ArticleMolecular and cellular biology1994
Functional differences between HOX proteins conferred by two residues in the homeodomain N-terminal arm.
Article in Molecular and cellular biology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 43 citations in OpenAlex.
- Diversification and Functional Evolution of HOX Proteins.Frontiers in cell and developmental biology · 2022Review
- Article
- HOX transcription factors are potential targets and markers in malignant mesothelioma.BMC cancer · 2016Article
- Article
- Hox transcription factors influence motoneuron identity through the integrated actions of both homeodomain and non-homeodomain regions.Developmental dynamics : an official publication of the American Association of Anatomists · 2012Article
- The truncated Hoxa1 protein interacts with Hoxa1 and Pbx1 in stem cells.Journal of cellular biochemistry · 2009Article
- HOX transcription factors are potential therapeutic targets in non-small-cell lung cancer (targeting HOX genes in lung cancer).British journal of cancer · 2009Article
- A mutation in HOXA2 is responsible for autosomal-recessive microtia in an Iranian family.American journal of human genetics · 2008Article
- Changing homeodomain residues 2 and 3 of Hoxa1 alters its activity in a cell-type and enhancer dependent manner.Nucleic acids research · 2002Article
- Characterization of Hoxd1 protein-DNA-binding specificity using affinity chromatography and random DNA oligomer selection.Cellular and molecular neurobiology · 2001Article
- The control of trunk Hox specificity and activity by Extradenticle.Genes & development · 1999Article
- HOXA9 forms triple complexes with PBX2 and MEIS1 in myeloid cells.Molecular and cellular biology · 1999Article
- Homeodomain-DNA interactions of the Pho2 protein are promoter-dependent.Nucleic acids research · 1997Article
- A molecular code dictates sequence-specific DNA recognition by homeodomains.The EMBO journal · 1996Article
- In the TTF-1 homeodomain the contribution of several amino acids to DNA recognition depends on the bound sequence.Nucleic acids research · 1996Article
- Repression by HoxA7 is mediated by the homeodomain and the modulatory action of its N-terminal-arm residues.Molecular and cellular biology · 1996Article
- An extradenticle-induced conformational change in a HOX protein overcomes an inhibitory function of the conserved hexapeptide motif.The EMBO journal · 1996Article
- Pbx modulation of Hox homeodomain amino-terminal arms establishes different DNA-binding specificities across the Hox locus.Molecular and cellular biology · 1996Article
- Cooperative interactions between HOX and PBX proteins mediated by a conserved peptide motif.Molecular and cellular biology · 1995Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hox genes encode homeodomain-containing transcriptional regulators that function during development to specify positional identity along embryonic axes. The homeodomain is composed of a flexible N-terminal arm and three alpha helices, and it differentially binds DNA. A number of homeodomains recognize sites containing a TAAT core motif. The product of the murine Hoxd-4 (Hox-4.2) gene functions in a positive autoregulatory fashion in P19 cells that is dependent on two TAAT motifs in the Hoxd-4 promoter. This effect is specific in that murine HOXA-1 (HOX-1.6) is unable to activate transcription through the Hoxd-4 autoregulatory element. Here we show that this is due to an inability of the HOXA-1 homeodomain to bind a HOXD-4 recognition site effectively. We have produced chimeras between HOXD-4 and HOXA-1 to map specific residues responsible for this functional difference. When positions 2 and 3 in the N-terminal arm of HOXA-1 were converted to HOXD-4 identity, both strong DNA binding and transcriptional activation were rescued. This substitution appears to confer an increased DNA-binding ability on the HOXA-1 homeodomain, since we were unable to detect a high-affinity recognition sequence for HOXA-1 in a randomized pool of DNA probes. The contribution of position 3 to DNA binding has been implicated by structural studies, but this is the first report of the importance of position 2 in regulating homeodomain-DNA interactions. Additionally, specific homeodomain residues that confer major differences in DNA binding and transcriptional activation between Hox gene products have not been previously determined. Identity at these two positions is generally conserved among paralogs but varies between Hox gene subfamilies. As a result, these residues may be important for the regulation of target gene expression by specific Hox products.
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