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Purification of the proline-rich homeodomain protein

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

Authors

Amy J. Butcher

Kevin Gaston

Padma-Sheela Jayaraman



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.

Journal Article Type Article
Publication Date Mar 25, 2003
Journal Journal of Chromatography B
Print ISSN 1570-0232
Publisher Elsevier
Peer Reviewed Peer Reviewed
Volume 786
Issue 1-2
Pages 3-6
Institution 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
DOI https://doi.org/10.1016/S1570-0232%2802%2900740-7
Publisher URL https://www.sciencedirect.com/science/article/pii/S1570023202007407


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