ArticleNucleic acids research1996
Hox homeodomain proteins exhibit selective complex stabilities with Pbx and DNA.
Article in Nucleic acids research, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed.
- PBX-dependent and independent Hox programs establish and maintain motor neuron terminal Identity.bioRxiv : the preprint server for biology · 2025Article
- Peptides as multifunctional players in cancer therapy.Experimental & molecular medicine · 2023Review
- A Computer-Based Methodology to Design Non-Standard Peptides Potentially Able to Prevent HOX-PBX1-Associated Cancer Diseases.International journal of molecular sciences · 2021Article
- 'Building a perfect body': control of vertebrate organogenesis by PBX-dependent regulatory networks.Genes & development · 2019Review
- Special AT-rich Sequence-binding Protein 1 (SATB1) Functions as an Accessory Factor in Base Excision Repair.The Journal of biological chemistry · 2016Article
- Pbx Regulates Patterning of the Cerebral Cortex in Progenitors and Postmitotic Neurons.Neuron · 2015Article
- CUX2 protein functions as an accessory factor in the repair of oxidative DNA damage.The Journal of biological chemistry · 2015Article
- The function of CUX1 in oxidative DNA damage repair is needed to prevent premature senescence of mouse embryo fibroblasts.Oncotarget · 2015Article
- Article
- HoxA9 regulated Bcl-2 expression mediates survival of myeloid progenitors and the severity of HoxA9-dependent leukemia.Oncotarget · 2013Article
- Review
- RARγ is essential for retinoic acid induced chromatin remodeling and transcriptional activation in embryonic stem cells.Journal of cell science · 2013Article
- Antisense oligonucleotide mediated knockdown of HOXC13 affects cell growth and induces apoptosis in tumor cells and over expression of HOXC13 induces 3D-colony formation.RSC advances · 2013Article
- Antagonism versus cooperativity with TALE cofactors at the base of the functional diversification of Hox protein function.PLoS genetics · 2013Article
- Homeodomain-containing protein HOXB9 regulates expression of growth and angiogenic factors, facilitates tumor growth in vitro and is overexpressed in breast cancer tissue.The FEBS journal · 2012Article
- Congenital diaphragmatic hernia candidate genes derived from embryonic transcriptomes.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Structural basis for sequence specific DNA binding and protein dimerization of HOXA13.PloS one · 2011Article
- Article
- HOXB13 is co-localized with androgen receptor to suppress androgen-stimulated prostate-specific antigen expression.Anatomy & cell biology · 2010Article
- Article
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9 authors.
Funding
Abstract
Eight of the nine homeobox genes of the Hoxb locus encode proteins which contain a conserved hexapeptide motif upstream from the homeodomain. All eight proteins (Hoxb-1-Hoxb-8) bind to a target oligonucleotide in the presence of Pbx1a under conditions where minimal or no binding is detected for the Hox or Pbx1a proteins alone. The stabilities of the Hox-Pbx1a-DNA complexes vary >100-fold, with the proteins from the middle of the locus (Hoxb-5 and Hoxb-6) forming very stable complexes, while Hoxb-4, Hoxb-7 and Hoxb-8 form complexes of intermediate stability and proteins at the 3'-side of the locus (Hoxb-1-Hoxb-3) form complexes which are very unstable. Although Hox-b proteins containing longer linker sequences between the hexapeptide and homeodomains formed unstable complexes, shortening the linker did not confer complex stability. Homeodomain swapping experiments revealed that this motif does not independently determine complex stability. Naturally occurring variations within the hexapeptides of specific Hox proteins also do not explain complex stability differences. However, two core amino acids (tryptophan and methionine) which are absolutely conserved within the hexapeptide domains appear to be required for complex formation. Removal of N- and C-terminal flanking regions did not influence complex stability and the members of paralog group 4 (Hoxa-4, b-4, c-4 and d-4), which share highly conserved hexapeptides, linkers and homeodomains but different flanking regions, form complexes of similar stability. These data suggest that the structural features of Hox proteins which determine Hox-Pbx1a-DNA complex stability reside within the precise structural relationships between the homeodomain, hexapeptide and linker regions.
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