Arginine methylation of HSP70 regulates retinoid acid-mediated RARβ2 gene activation

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 112; no. 26; pp. E3327 - E3336
• Main Authors: Gao, Wei-wei, Xiao, Rong-quan, Peng, Bing-ling, Xu, Huan-teng, Shen, Hai-feng, Huang, Ming-feng, Shi, Tao-tao, Yi, Jia, Zhang, Wen-juan, Wu, Xiao-nan, Gao, Xiang, Lin, Xiang-zhi, Dorrestein, Pieter C., Rosenfeld, Michael G., Liu, Wen
• Format: Journal Article
• Language: English
• Published: United States National Acad Sciences 30.06.2015; National Academy of Sciences
• Series: PNAS Plus
• Subjects: Amino Acid Sequence; arginine; Arginine - metabolism; Biological Sciences; chromatin; Chromatin - metabolism; gene activation; Gene Expression Regulation; genes; HEK293 Cells; HSP70 Heat-Shock Proteins - chemistry; HSP70 Heat-Shock Proteins - metabolism; Humans; Methylation; molecular chaperones; Molecular Sequence Data; PNAS Plus; protein folding; quality control; Receptors, Retinoic Acid - genetics; transcription (genetics); Transcription Factor TFIIH - metabolism; Transcription, Genetic; Tretinoin - pharmacology; arginine methylation; heat-shock proteins; gene transcription

HSP70 proteins are well known as molecular chaperones involved in protein folding and quality control. Whether they also function in gene transcription on chromatin, and if so, how they are regulated, remains elusive. Here we report that HSP70 can also regulate gene transcription through its associa...