Histone tyrosine sulfation by SULT1B1 regulates H4R3me2a and gene transcription.

Nature chemical biology 2023 Jul

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Tyrosine sulfation is a common posttranslational modification in mammals. To date, it has been thought to be limited to secreted and transmembrane proteins, but little is known about tyrosine sulfation on nuclear proteins. Here we report that SULT1B1 is a histone sulfotransferase that can sulfate the tyrosine 99 residue of nascent histone H3 in cytosol. The sulfated histone H3 can be transported into the nucleus and majorly deposited in the promoter regions of genes in chromatin. While the H3Y99 residue is buried inside octameric nucleosome, dynamically regulated subnucleosomal structures provide chromatin-H3Y99sulf the opportunity of being recognized and bound by PRMT1, which deposits H4R3me2a in chromatin. Disruption of H3Y99sulf reduces PRMT1 binding to chromatin, H4R3me2a level and gene transcription. These findings reveal the mechanisms underlying H3Y99 sulfation and its cross-talk with H4R3me2a to regulate gene transcription. This study extends the spectrum of tyrosine sulfation on nuclear proteins and the repertoire of histone modifications regulating chromatin functions. © 2023. The Author(s), under exclusive licence to Springer Nature America, Inc.

Citation

Weixing Yu, Runxin Zhou, Nan Li, Zhi-Chao Lei, Dingyuan Guo, Fei Peng, Yan Li, Xue Bai, Shan Feng, Yu Wang, Jie He, Sibi Yin, Xiao Zeng, Leya He, Yuan Gao, Mingchang Li, Yusong R Guo, Ke Liu, Yugang Wang. Histone tyrosine sulfation by SULT1B1 regulates H4R3me2a and gene transcription. Nature chemical biology. 2023 Jul;19(7):855-864