@article{Methacryllysine:2232,
      recid = {2232},
      author = {Delaney, Kyle Adam},
      title = {Discovery and Validation of Methacryllysine Modification  on Histone Proteins},
      publisher = {University of Chicago},
      school = {Ph.D.},
      address = {2020-06},
      pages = {160},
      abstract = {In recent years, a variety of new posttranslational  protein modifications occurring on histone proteins have  been discovered. This includes lysine crotonylation, an  enzymatically regulated epigenetic histone mark. Here we  report the discovery of a new type of posttranslational  modification occurring on histones, lysine methacrylation.  Methacryllysine is a structural isomer of crotonyllysine.  We validated the identity of the modification using mass  spectrometry for co-elution, ozonolysis, and isotopic  labeling experiments. We generated and validated pan  specific and site specific antibodies for this mark. We  report that HAT1 can enzymatically catalyze the addition of  this modification, representing the first published report  of HAT1 using a substrate other than acetyl-CoA. Here we  also provide the first report that SIRT1 and SIRT2 catalyze  the removal of this modification.},
      url = {http://knowledge.uchicago.edu/record/2232},
      doi = {https://doi.org/10.6082/uchicago.2232},
}