Tandem Histone-Binding Domains Enhance the Activity of a Synthetic Chromatin Effector.

ABSTRACT: Fusion proteins that specifically interact with biochemical marks on chromosomes represent a new class of synthetic transcriptional regulators that decode cell state information rather than DNA sequences. In multicellular organisms, information relevant to cell state, tissue identity, and oncogenesis is often encoded as biochemical modifications of histones, which are bound to DNA in eukaryotic nuclei and regulate gene expression states. We have previously reported the development and validation of the "polycomb-based transcription factor" (PcTF), a fusion protein that recognizes histone modifications through a protein-protein interaction between its polycomb chromodomain (PCD) motif and trimethylated lysine 27 of histone H3 (H3K27me3) at genomic sites. We demonstrated that PcTF activates

SUBMITTER: Tekel SJ 

PROVIDER: S-EPMC8928417 | biostudies-literature | 2018 Mar

REPOSITORIES: biostudies-literature