The PR domain of the Rb-binding zinc finger protein RIZ1 is a protein binding interface and is related to the SET domain functioning in chromatin-mediated gene expression.

The Journal of Biological Chemistry
S HuangL Liu

Abstract

The PR domain, first noted as the PRDI-BF1-RIZ1 homologous region, defines a sub-class of zinc finger genes that appear to function as negative regulators of tumorigenesis. This family includes the MDS1-EVI1 gene inactivated in myeloid leukemia, the PRDI-BF1/BLIMP1 transcription repressor of c-myc involved in driving B-cell differentiation, and the RIZ gene, which encodes proteins capable of binding to the retinoblastoma tumor suppressor protein (Rb). The PR domain of MDS1-EVI1 is disrupted by translocations linked to myeloid leukemia, resulting in the activation of the PR-minus oncogenic product EVI1. Remarkably similar to MDS1-EVI1, RIZ gene also normally produces two protein products of different length, and the smaller protein RIZ2 lacks the PR domain of RIZ1 but is otherwise identical to RIZ1. These observations raise considerable interest to determine the function of PR. We show here that RIZ1 PR domain mediates protein-protein interaction. Recombinant fusion proteins of PR can bind to in vitro translated RIZ1 and RIZ2 proteins. The binding can be disrupted by amino acid substitutions at conserved residues of PR, suggesting that binding is specific. Of the three conserved exons of PR, the first two appear dispensable for ...Continue Reading

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