Poster abstracts
Poster number 35 submitted by Liudmila Popova
Utilizing proximity-dependent labeling methods to identify proteins proximal to Hat1 in vivo.
Liudmila Popova (MCBD), Miranda Gardner (OSBP), Michael Freitas, PhD (Department of Cancer Biology and Genetics), Mark Parthun, PhD (Department of Biomedical Chemistry and Pharmacology)
Abstract:
Histone acetyltransferase 1 (Hat1) is an enzyme known to acetylate Lysines 5 and 12 on the tail of the newly synthesized histone H4 during the process of replication-coupled chromatin assembly. In addition, Hat1 has been suggested to play a role in eukaryotic DNA damage response by being involved in the repair of DNA double-strand breaks. In an attempt to learn more about the cellular roles of Hat1, our lab utilized a proximity-dependent biotin identification approach (BioID) to isolate proteins that in vivo are proximal Hat1. Coupling this methodology to mass spectrometry has led to identification of a number of vicinal proteins. Current work is focused on utilizing another proximity-based labeling technique, APEX2 to find proteins that are in vivo proximal to Hat1.
References:
Parthun, M.R. Hat1: the emerging cellular roles of a type B histone acetyltransferase. Oncogene. 2007; 26, 5319-28.
Lambert, J.P. et al. Proximity biotinylation and affinity purification are complementary approaches for the interactome mapping of chromatin-associated protein complexes. J Proteomics. 2015 Apr 6;118:81-94.
Martell, J.D. et al. Electron microscopy using the genetically encoded APEX2 tag in cultured mammalian cells. Nat Protoc. 2017 Sep;12(9):1792-1816.
Keywords: Hat1, BioID, APEX2