SAFB1 interacts with and suppresses the transcriptional activity of p53

Abstract

A significant amount of nuclear p53 is found associated with the nuclear matrix in cells that were exposed to genotoxic stress. In this study we identified Scaffold attachment factor B1 (SAFB1), a nuclear matrix-associated protein that binds the scaffold or matrix attachment regions (S/MARs) of genomic DNA, as a novel p53-interacting protein. SAFB1 was able to associate with p53 through its C-terminal domain, while significant co-localization of the two proteins was observed in cells treated with 5-fluorouracil or mithramycin. Binding of p53 to SAFB1 had a significant functional outcome, since SAFB1 was shown to suppress p53-mediated reporter gene expression. These data suggest that nuclear matrix-associated proteins may play a critical role in regulating p53 localization and activity. Structured summary: p53 physically interacts with SRPK1a:shown by two hybrid (view interaction) p53 physically interacts with SRPK1a:shown by pull down (view interaction) p53 physically interacts with SRPK1a:shown by anti bait coimmunoprecipitation (view interaction) p53 physically interacts with SRPK1a:shown by anti tag coimmunoprecipitation (view interaction) SAFB1 physically interacts with p53:shown by pull down (view interactions 1, 2) SAFB1 physically interacts with p53:shown by anti bait coimmunoprecipitation (view interactions 1, 2) SAFB1 and p53 colocalize:shown by fluorescence microscopy (view interaction) SAFB2 physically interacts with p53:shown by pull down (view interaction) (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.