@article{TEXTUAL,
      recid = {11022},
      author = {Huang, He and Zhang, Di and Weng, Yejing and Delaney, Kyle  and Tang, Zhanyun and Yan, Cong and Qi, Shankang and Peng,  Chao and Cole, Philip A. and Roeder, Robert G. and Zhao,  Yingming},
      title = {The regulatory enzymes and protein substrates for the  lysine β-hydroxybutyrylation pathway},
      journal = {Science Advances},
      address = {2021-02-24},
      number = {TEXTUAL},
      abstract = {Metabolism-mediated epigenetic changes represent an  adapted mechanism for cellular signaling, in which lysine  acetylation and methylation have been the historical focus  of interest. We recently discovered a  β-hydroxybutyrate-mediated epigenetic pathway that couples  metabolism to gene expression. However, its regulatory  enzymes and substrate proteins remain unknown, hindering  its functional study. Here, we report that the  acyltransferase p300 can catalyze the enzymatic addition of  β-hydroxybutyrate to lysine (Kbhb), while histone  deacetylase 1 (HDAC1) and HDAC2 enzymatically remove Kbhb.  We demonstrate that p300-dependent histone Kbhb can  directly mediate in vitro transcription. Moreover, a  comprehensive analysis of Kbhb substrates in mammalian  cells has identified 3248 Kbhb sites on 1397 substrate  proteins. The dependence of histone Kbhb on p300 argues  that enzyme-catalyzed acylation is the major mechanism for  nuclear Kbhb. Our study thus reveals key regulatory  elements for the Kbhb pathway, laying a foundation for  studying its roles in diverse cellular processes.},
      url = {http://knowledge.uchicago.edu/record/11022},
}