Production of mouse Hox-2.1 protein in Escherichia coli: characterisation of in vitro binding to DNA.
The developmentally regulated mouse Hox-2.1 gene encodes a homeodomain-containing (Hox) protein which is likely to function as a transcription factor. We expressed the DNA coding for full-length Hox-2.1 protein in a T7 promoter-containing vector in bacteria, which produced low levels of protein showing weak DNA-binding activity. Synthesis of a truncated polypeptide lacking all the sequence upstream from the homeodomain enabled us to produce greater amounts of protein and demonstrate its sequence-dependent DNA binding. The tetranucleotide ATTA is necessary for binding, but a single copy is not by itself sufficient. Flanking sequences are important; in particular a cytosine immediately 5' to the ATTA enhances binding.[1]References
- Production of mouse Hox-2.1 protein in Escherichia coli: characterisation of in vitro binding to DNA. Budd, P.S., Jackson, I.J. Gene (1991) [Pubmed]
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