title: Purification of the proline-rich homeodomain protein.
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.
authors.affiliation: Department of Biochemistry, School of Medical Sciences, University Walk, University of Bristol, Bristol, UK BS8 1TD.
authors.forename: Amy J
authors.initials: AJ
authors.lastname: Butcher
authors.forename: Kevin
authors.initials: K
authors.lastname: Gaston
authors.forename: Padma-Sheela
authors.initials: PS
authors.lastname: Jayaraman
mesh_terms: D001483:Base Sequence; D017931:DNA Primers; D004591:Electrophoresis, Polyacrylamide Gel; D018398:Homeodomain Proteins / Q000302:isolation & purification*; D010455:Peptides / Q000302:isolation & purification*; D055232:Proline-Rich Protein Domains
chemical_list: D017931:DNA Primers; D018398:Homeodomain Proteins; D010455:Peptides