Differential DNA binding properties of three human homeodomain proteins
| Autor: | Antonio Simeone, Lorenza Sanseverino, Maria Teresa Corsetti, Paola Briata, Antonio Daga, Irma Airoldi, Giulio Palmisano, Giorgio Corte, Edoardo Boncinelli, Cristiano Angelini |
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| Rok vydání: | 1992 |
| Předmět: |
Glycosylation
Insecta animal structures Molecular Sequence Data Biology Genetics Animals Humans Cloning Molecular Binding site Promoter Regions Genetic Hox gene Gene Transcription factor Cells Cultured Base Sequence Genes Homeobox Promoter Molecular biology Recombinant Proteins Cell biology DNA-Binding Proteins Kinetics Oligodeoxyribonucleotides Regulatory sequence Multigene Family embryonic structures Homeobox Homeotic gene Baculoviridae Transcription Factors |
| Zdroj: | Scopus-Elsevier |
| ISSN: | 1362-4962 0305-1048 |
| DOI: | 10.1093/nar/20.17.4465 |
| Popis: | The products of three human homeobox containing (HOX) genes, 2C, 3C and 4B, were produced in insect cells using the Baculovirus expression system and purified to near homogeneity. In this system we observed that the DNA binding forms of the three proteins are not glycosylated. HOX 3C and 4B are phosphorylated in insect cells, while HOX 2C is not. The three HOX proteins bind to a DNA sequence known to be a target site for Antennapedia protein with a very similar affinity (Kd = 1-2 x 10(-9) M). We then measured their binding properties to four human sequences present in the HOX 3D, 4C, 1C and 4B promoters. Two of these sequences have been reported to be binding sites for HOX proteins. HOX 2C, 3C and 4B behaved quite differently, showing low affinity for promoters of genes located upstream from their own gene in the HOX clusters and a higher affinity for regulatory sequences of their own gene and downstream HOX genes. |
| Databáze: | OpenAIRE |
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