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Arginine methylation of hnRNP K enhances p53 transcriptional activity
Author(s) -
Chen Yibin,
Zhou Xinyuan,
Liu Na,
Wang Chaochen,
Zhang Liang,
Mo Wei,
Hu Gengxi
Publication year - 2008
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.04.051
Subject(s) - methylation , arginine , dna methylation , microbiology and biotechnology , chemistry , dna , biology , biochemistry , gene expression , amino acid , gene
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.