Refined read-out: hUHRF1-tandem Tudor prefers histone H3 containing K9me2/3 and K4me1

Histone post-translational modifications (PTMs) are an important part of chromatin signaling mechanisms. Among them, histone H3 has a prominent role, and combinations of multiple PTMs are common. We investigated binding of multiple marks on the same H3 histone by the human UHRF1-TTD (Uniprot Q96T88, residues 126-280), known to bind H3K9me2/3 histones. We verified binding to H3K9me2/3 and demonstrated stronger binding to synthetic H3 peptides containing K4me1 and K9me2/3 as well as native HepG2 mononucleosomes bearing both H3K9me2/3 and H3K4me1. Overall design: CIDOP (ChIP-like) pulldown of HepG2 native mononucleosomes with hUHRF1-TTD (GST-tagged).