The Abd-B-like Hox Homeodomain Proteins Can Be Subdivided by the Ability to Form Complexes with Pbx1a on a Novel DNA Target
| Autor: | Corey Largman, H. Jeffrey Lawrence, Wei-Fang Shen, S Rozenfeld |
|---|---|
| Rok vydání: | 1997 |
| Předmět: |
animal structures
Molecular Sequence Data Xenopus Proteins Biology Biochemistry DNA sequencing Structure-Activity Relationship chemistry.chemical_compound Proto-Oncogene Proteins Drosophila Proteins Humans Amino Acid Sequence Binding site Hox gene Molecular Biology Homeodomain Proteins Genetics chemistry.chemical_classification Base Sequence Pre-B-Cell Leukemia Transcription Factor 1 fungi Genes Homeobox Tryptophan Cooperative binding DNA Cell Biology TATA Box Amino acid DNA-Binding Proteins Homeobox A10 Proteins chemistry embryonic structures Homeobox Transcription Factors |
| Zdroj: | Journal of Biological Chemistry. 272:8198-8206 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.272.13.8198 |
| Popis: | Previous studies showed that the Hox homeodomain proteins from paralog groups 1-8 display cooperative DNA binding with the non-Hox homeodomain protein Pbx, mediated by a canonical YPWM. Although the Abd-B-like Hox proteins in paralogs 9-13 lack this sequence, Hoxb-9 and Hoxa-10 were reported to bind with Pbx1a to DNA. We show that these interactions require a tryptophan 6 amino acids N-terminal to the homeodomain. Binding site selection for Hoxb-9 with Pbx1a yielded ATGATTTACGAC, containing a novel TTAC Hox-binding site adjacent to a Pbx site. In the presence of Pbx1a, Hoxb-9 and Hoxa-10 bound to targets containing either TTAC or TTAT. These data extend previous findings that interactions with Pbx define a Hox protein binding code for different DNA sequences across paralog groups 1 through 10. Members of the 11, 12, and 13 paralogs do not cooperatively bind DNA with Pbx1a, despite the presence of tryptophan residues N-terminal to the homeodomain in Hoxd-12 and Hoxd-13. Hoxa-11, Hoxd-12, or Hoxd-13, in the presence of Pbx1a, selected a TTAC Hox site but lacking a Pbx1a site. These data suggest that Abd-B-like Hox proteins bind to a novel TTAC site and can be divided by their cooperative binding to DNA with Pbx1a. |
| Databáze: | OpenAIRE |
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