Abstract
The proline-rich homeodomain protein (PRH), also known as Hex, is a transcriptional repressor expressed in a variety of cell types. The PRH protein contains a proline-rich N-terminal domain that can repress transcription when attached to a heterologous DNA binding domain, a central homeodomain that mediates sequence-specific DNA binding, and an acidic C-terminal domain of unknown function. Although individual domains of PRH have been expressed in bacterial cells as GST- and histidine-tagged fusion proteins, attempts to express and purify the full-length protein have met with little success. Here we describe the purification of a histidine-tagged full-length PRH fusion protein. The protein described here will allow us to determine the mechanisms whereby PRH represses transcription.
Original language | English |
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Pages (from-to) | 3-6 |
Number of pages | 4 |
Journal | Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences |
Volume | 786 |
Issue number | 1-2 |
Publication status | Published - 25 Mar 2003 |
Keywords
- Base Sequence
- DNA Primers
- Electrophoresis, Polyacrylamide Gel
- Homeodomain Proteins
- Peptides
- Proline-Rich Protein Domains