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Updated: Aug 16, 2026

Purification of Hsp104, a Protein Disaggregase
Published on: September 30, 2011
Purification of the proline-rich homeodomain protein
Amy J Butcher1, Kevin Gaston, Padma-Sheela Jayaraman
1Department of Biochemistry, School of Medical Sciences, University Walk, University of Bristol, Bristol, UK BS8 1TD.
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.
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