Department of Chemistry, Aristotle University of Thessaloniki, Thessaloniki, Greece.
FEBS Lett. 2011 Jan 3;585(1):78-84. doi: 10.1016/j.febslet.2010.11.054. Epub 2010 Dec 3.
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.
大量核 p53 存在于受到遗传毒性应激的细胞的核基质中。在本研究中，我们鉴定了支架附着因子 B1（SAFB1），一种与基因组 DNA 的支架或基质附着区（S/MARs）结合的核基质相关蛋白，为一种新的 p53 相互作用蛋白。SAFB1 能够通过其 C 末端结构域与 p53 结合，而在用 5-氟尿嘧啶或米托蒽醌处理的细胞中观察到两种蛋白的明显共定位。p53 与 SAFB1 的结合具有显著的功能结果，因为 SAFB1 被证明可以抑制 p53 介导的报告基因表达。这些数据表明，核基质相关蛋白可能在调节 p53 定位和活性方面发挥关键作用。
