The DNA binding specificity of ultrabithorax is modulated by cooperative interactions with extradenticle, another homeoprotein

@article{Chan1994TheDB,
  title={The DNA binding specificity of ultrabithorax is modulated by cooperative interactions with extradenticle, another homeoprotein},
  author={S K Chan and Leah Jaffe and Maria Capovilla and Juan Botas and Richard S. Mann},
  journal={Cell},
  year={1994},
  volume={78},
  pages={603-615}
}
The Ultrabithorax (Ubx) and Antennapedia (Antp) genes of Drosophila encode homeodomain proteins that have very similar DNA binding specificities in vitro but specify the development of different segmental patterns in vivo. We describe cooperative interactions between Ubx protein and a divergent homeodomain protein, extradenticle (exd), that selectively increases the affinity of Ubx, but not Antp, for a particular DNA target. We also provide evidence that Ubx and exd bind to neighboring sites on… Expand

Topics from this paper

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TLDR
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TLDR
A novel and evolutionarily conserved mechanism for regulating HOX activity in which a direct protein-protein interaction between EXD and HTH results in EXD's nuclear translocation is suggested. Expand
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TLDR
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TLDR
It is reported that the regulation of a newly identified Lab target gene does not rely on the previously established consensus Lab/Exd/Hth-binding site, but on a strongly divergent sequence, suggesting that Lab, and most probably other Hox proteins, selects different DNA sequences in regulating downstream target genes. Expand
Chromosomal binding sites of Ultrabithorax homeotic proteins
TLDR
The binding sites of Ubx proteins (UBX) in polytene chromosomes are mapped and it is found that the UBX isoforms Ia and IVa accumulate in about 100 discrete chromosomal sites. Expand
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References

SHOWING 1-10 OF 50 REFERENCES
Functional specificity of the Antennapedia homeodomain.
TLDR
The three-dimensional structure of the Antp homeodomain-DNA complex shows that this N-terminal arm is located in the minor groove of the DNA, suggesting that the functional specificity is determined either by slight differences in DNA binding and/or by selective interactions with other transcription factor(s). Expand
Immunochemical dissection of the Ultrabithorax homeoprotein family in Drosophila melanogaster.
  • A. J. Lopez, D. Hogness
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
  • 1991
TLDR
Results support the hypothesis that alternative splicing and phosphorylation modulate developmentally specific functions of the Ubx gene and suggest that Ultrabithorax proteinosphorylation is also developmentally regulated. Expand
The sequence specificity of homeodomain-DNA interaction
TLDR
The similarity in sequence specificity of En and Ftz HDs suggests that, within families of DNA binding proteins, close relatives will exhibit similar specificities, and competition among related regulatory proteins might govern which protein occupies a given binding site and consequently determine the ultimate effect of cis-acting regulatory sites. Expand
Cooperative interactions between the Caenorhabditis elegans homeoproteins UNC-86 and MEC-3.
TLDR
The POU-type homeodomain protein UNC-86 and the MEC-3, which specify neuronal cell fate in the nematode Caenorhabditis elegans, bind cooperatively as a heterodimer to the mec-3 promoter, increasing DNA binding stability and, therefore, increases DNA binding specificity. Expand
Antp‐type homeodomains have distinct DNA binding specificities that correlate with their different regulatory functions in embryos.
TLDR
The good correlation between the in vitro DNA binding preferences of these four Antp‐type homeodomain proteins and their ability to specifically regulate a Dfd enhancer element in the embryo, suggests that the modest binding differences that distinguish them make an important contribution to their unique regulatory specificities. Expand
Differential DNA sequence recognition is a determinant of specificity in homeotic gene action.
TLDR
It is shown here that the homeodomains encoded by the Ultrabithorax and Deformed homeotic genes bind optimally to distinct DNA sequences and have mapped the determinants responsible for differential recognition. Expand
The segment identity functions of Ultrabithorax are contained within its homeo domain and carboxy-terminal sequences.
TLDR
The structural differences that distinguish two Drosophila homeotic selector proteins, Ultrabithorax (Ubx) and Antennapedia (Antp), have been investigated and it is demonstrated that the assay used to measure the segment identity functions of Ubx and Antp is independent of any homeotic gene normally active in thoracic and abdominal segments. Expand
Functional dissection of ultrabithorax proteins in D. melanogaster
TLDR
Analysis of the transformations generated by UBx deletions and by a chimeric Ultrabithorax-Antennapedia protein demonstrated that the majority of the UBX identity information is contained within the C-terminal, homeodomain-containing portion of the protein. Expand
Direct regulation of decapentaplegic by Ultrabithorax and its role in Drosophila midgut morphogenesis
TLDR
It is shown that Ubx directly regulates dpp expression, a 674 bp enhancer of dpp controlling its expression in the second constriction domain of the visceral mesoderm (parasegment 7), and these regulatory interactions are relevant to normal development. Expand
A short, disordered protein region mediates interactions between the homeodomain of the yeast α2 protein and the MCM1 protein
TLDR
It is shown that correct target site selection by the yeast alpha 2 protein requires, as well as its homeodomain, an adjacent short and apparently unstructured region of the protein. Expand
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