Purification of the proline-rich homeodomain protein

Amy J Butcher, Kevin Gaston, Padma-Sheela Jayaraman

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)


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 languageEnglish
Pages (from-to)3-6
Number of pages4
JournalJournal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences
Issue number1-2
Publication statusPublished - 25 Mar 2003


  • Base Sequence
  • DNA Primers
  • Electrophoresis, Polyacrylamide Gel
  • Homeodomain Proteins
  • Peptides
  • Proline-Rich Protein Domains


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