SUMO-1 modification regulates the DNA binding activity of heat shock transcription factor 2, a promyelocytic leukemia nuclear body associated transcription factor
SUMO-1 modification regulates the DNA binding activity of heat shock transcription factor 2, a promyelocytic leukemia nuclear body associated transcription factor
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DOI：
10.1074/jbc.m008066200
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发表时间：
2001-05-25
影响因子：
4.8
通讯作者：
Sarge, KD
中科院分区：
文献类型：
--
作者：
Goodson, ML;Hong, Y;Sarge, KD
热休克转录因子2（HSF 2）是一种调节热休克蛋白基因表达的转录因子，但其调控机制尚不清楚。本文报道HSF 2是泛素相关蛋白SUMO-1修饰的底物，并与SUMO-1共定位于细胞核颗粒中。用抗早幼粒细胞白血病抗体染色表明，这些含HSF 2的核颗粒是PML小体。我们的研究结果确定赖氨酸82作为SUMO-1在HSF 2中修饰的主要位点，其位于该蛋白质的DNA结合结构域内的“翼”。有趣的是，HSF 2的SUMO-1修饰导致该因子转化为活性DNA结合形式。这是首次证明SUMO-1修饰可以直接改变转录因子的DNA结合能力，并揭示了SUMO-1修饰可以调节蛋白质功能的新机制。
Heat shock transcription factor 2 (HSF2) is a transcription factor that regulates heat shock protein gene expression, but the mechanisms regulating the function of this factor are unclear, Here we report that HSF2 is a substrate for modification by the ubiquitin-related protein SUMO-1 and that HSF2 colocalizes in cells with SUMO-1 in nuclear granules. Staining with anti-promyelocytic leukemia antibodies indicates that these HSF2-containing nuclear granules are PML bodies. Our results identify lysine 82 as the major site of SUMO-1 modification in HSF2, which is located in a "wing" within the DNA-binding domain of this protein. Interestingly, SUMO-1 modification of HSF2 results in conversion of this factor to the active DNA binding form. This is the first demonstration that SUMO-1 modification can directly alter the DNA binding ability of a transcription factor and reveals a new mechanism by which SUMO-1 modification can regulate protein function.