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首页> 外文期刊>Journal of Molecular Biology >SUMOylation of the lens epithelium-derived growth factor/p75 attenuates its transcriptional activity on the heat shock protein 27 promoter.
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SUMOylation of the lens epithelium-derived growth factor/p75 attenuates its transcriptional activity on the heat shock protein 27 promoter.

机译：晶状体上皮来源的生长因子/ p75的SUMOylation减弱了其对热激蛋白27启动子的转录活性。

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摘要

Lens epithelium-derived growth factor (LEDGF) proteins p75 and p52 are transcriptional coactivators that connect sequence-specific activators to the basal transcription machinery. We have found that these proteins are posttranslationally modified by SUMO (small ubiquitin-like modifier)-1 and SUMO-3. Three SUMOylation sites, K75, K250, and K254, were mapped on the shared N-terminal region of these molecules, while a fourth site, K364, was identified in the C-terminal part exclusive of LEDGF/p75. The N-terminal SUMO targets are located in evolutionarily conserved charge-rich regions that lack resemblance to the described consensus SUMOylation motif, whereas the C-terminal SUMO target is solvent exposed and situated in a typical consensus motif. SUMOylation did not affect the cellular localization of LEDGF proteins and was not necessary for their chromatin-binding ability, nor did it affect this activity. However, lysine to arginine mutations of the identified SUMO acceptor sites drastically inhibited LEDGF SUMOylation, extended the half-life of LEDGF/p75, and significantly increased its transcriptional activity on the heat shock protein 27 promoter, indicating a negative effect of SUMOylation on the transcriptional activity of LEDGF/p75. Considering that SUMOylation is known to negatively affect the transcriptional activity of all transcription factors known to transactivate heat shock protein 27 expression, these findings support the paradigm establishing SUMOylation as a global neutralizer of cellular processes upregulated upon cellular stress.
机译：晶状体上皮来源的生长因子（LEDGF）蛋白p75和p52是转录共激活因子，可将序列特异性激活因子连接至基础转录机制。我们发现这些蛋白质被SUMO（小的泛素样修饰剂）-1和SUMO-3进行了翻译后修饰。三个SUMOylation位点K75，K250和K254被定位在这些分子的共享N端区域，而在LEDGF / p75的C端部分发现了第四个位点K364。 N末端SUMO靶标位于与所述共有SUMOylation基序相似的进化保守的电荷丰富区域中，而C末端SUMO靶标是溶剂暴露的且位于典型的共有基序中。 SUMOylation不会影响LEDGF蛋白的细胞定位，对于其染色质结合能力不是必需的，也不会影响该活性。但是，已确定的SUMO受体位点的赖氨酸突变为精氨酸会极大地抑制LEDGF SUMO酰化，延长LEDGF / p75的半衰期，并显着增加其对热休克蛋白27启动子的转录活性，表明SUMOylation对转录的负面影响LEDGF / p75的活性。考虑到已知SUMOylation会负面影响已知可激活热休克蛋白27表达的所有转录因子的转录活性，因此这些发现支持建立SUMOylation作为细胞应激后上调的细胞过程的整体中和剂的范例。

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