Chen Yibin, Zhou Xinyuan, Liu Na, Wang Chaochen, Zhang Liang, Mo Wei, Hu Gengxi
State Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China.
FEBS Lett. 2008 May 28;582(12):1761-5. doi: 10.1016/j.febslet.2008.04.051. Epub 2008 May 8.
Previous studies have illustrated that hnRNP K, which could be methylated at arginine residues, plays a key role in coordinating transcriptional responses to DNA damage as a cofactor for p53. In this study, we observed that hnRNP K was markedly arginine methylated in response to UV radiation. Furthermore, arginine methylation of hnRNP K enhanced its affinity with p53. Inhibition of methylation in hnRNP K attenuated the recruitment of p53 to p21 promoter, and reduced p53 transcriptional activity. These data suggested that arginine methylation of hnRNP K is a key element for p53 transcriptional activity.
先前的研究表明，可在精氨酸残基处发生甲基化的异质性核糖核蛋白K（hnRNP K）作为p53的辅因子，在协调对DNA损伤的转录反应中起关键作用。在本研究中，我们观察到hnRNP K在紫外线辐射下精氨酸甲基化显著增加。此外，hnRNP K的精氨酸甲基化增强了其与p53的亲和力。抑制hnRNP K的甲基化会减弱p53向p21启动子的募集，并降低p53的转录活性。这些数据表明，hnRNP K的精氨酸甲基化是p53转录活性的关键因素。
