Purification of the proline-rich homeodomain protein

Butcher, Amy J.; Gaston, Kevin; Jayaraman, Padma-Sheela

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.

Citation

Butcher, A. J., Gaston, K., & Jayaraman, P. (2003). Purification of the proline-rich homeodomain protein. Journal of Chromatography B, 786(1-2), 3-6. doi:10.1016/S1570-0232(02)00740-7

• Journal Article Type: Article
• Acceptance Date: Jun 1, 2002
• Online Publication Date: Oct 16, 2002
• Publication Date: Mar 25, 2003
• Deposit Date: Nov 6, 2018
• Journal: Journal of Chromatography B
• Print ISSN: 1570-0232
• Publisher: Elsevier
• Peer Reviewed: Peer Reviewed
• Volume: 786
• Issue: 1-2
• Pages: 3-6
• DOI: https://doi.org/10.1016/S1570-0232%2802%2900740-7
• Public URL: https://nottingham-repository.worktribe.com/output/1037795
• Publisher URL: https://www.sciencedirect.com/science/article/pii/S1570023202007407