The study found that UHRF1, an E3 ubiquitin ligase, regulates DNA methylation through its association with histone H3 methylated at lysine 9 (H3K9). Using advanced peptide arrays technology featured in the HTPSA Core Facility, Dr. Strahl’s group found that UHRF1 association with H3K9 methylation can occur during mitosis – a cell cycle stage wherein other H3K9 methylation binders are normally ejected. The collective studies showed that UHRF1 mitotic binding to chromatin is necessary for DNA methylation maintenance through regulation of the stability of the enzyme that methylates DNA. This work is significant because it connects the regulation of two fundamentally important epiegentic marks together in humans. Furthermore, it shows how peptides and peptide arrays can be a useful tool for the investigation of biologically important protein-protein interactions.
The HTPSA Core Facility helped this study by providing high quality peptides and peptide arrays. The facility can help in design and synthesis of peptides for antibody production, Fluorescence Polarization assays, NMR and crystallography. The core has experience in fast synthesis of simple peptides and synthesis of peptides containing multiple tags and/or modifications, including phosphopeptides, fluorescent peptides, biotinylated peptides, peptides with post-translational modifications, and peptides with unnatural amino acids.
If you thinking about using peptides in your research, contact the HTPSA Core to discuss the optimal peptide design, advantages and disadvantages of using peptides, and answer your questions about peptide stability, handling and storage. For more information, visit the HTPSA Core Facility Website or email us at email@example.com