How the genetic code, in the form of DNA, is packaged into cells is not well understood. Many studies have found that DNA packaging is mediated through the actions of histone proteins that spool the DNA into structures called nucleosomes. While histones are responsible for DNA packaging, it turns out that chemical modifications or molecular tags on the histones provide the key instructions for how DNA becomes packed or opened up for functions like the expression of genes. A mystery in understanding how the chemical histone tags function has been the identification of the proteins these tags recruit. In this study, we set out to analyzed a large family of proteins that recognizes these histone modifications, plant homeodomains (PHDs). We have studied 123 PHD proteins with respect to their binding interactions with chemical histone tags and thoroughly described binding preference for 31 histone H3 binding PHDs in the context of various modifications (i.e. methylation, acetylation, phosphorylation, etc.). By using high-throughput arraying methods and sensitive proximity-based binding assays, this work provides a large database of information with respect to how PHDs interact with histones and their chemical tags.
A study of the epigenetic effector proteins, Plant Homeodomains (PHDs), from Dr. Brian D. Strahl’s lab titled “Characterization of the plant homeodomain (PHD) reader family for their histone tail interactions,” was published in Epigenetics & Chromatin on January 24th, 2020 (https://doi.org/10.1186/s13072-020-0328-z). The work was authored by Dr. Kanishk Jain, a postdoctoral trainee in Dr. Brian D. Strahl’s lab, and collaborators from Dr. Mark T. Bedford’s lab at MD Anderson and EpiCypher Inc.