16 October, 2020
The ability to discriminate between protein-DNA and protein-RNA interactions in complex cell extract mixtures has always presented a challenge for chromatin biochemists. As co-author in this publication, resulting from our collaborative project with the laboratory of Prof Henning Urlaub, Sebastian David presents a new mass spectrometry-based workflow to detect UV-induced cross-links between deoxyribonucleotides and proteins at single amino acid level. "To set up the novel technique, we have used recombinant mononucleosomes and chromatin arrays, linker histones and other DNA-binding proteins. The optimized protocol was then used to examine direct protein-DNA interactions in isolated HeLa nuclei. Besides its usefulness in mapping protein-DNA contacts, the technique also has the ability to specify if binding occurs on the nucleobase or the deoxyribose, which was used to distinguish between two binding modes of SCML2 to the nucleosome, in the presence or absence of linker histones. We are pleased to have contributed to this manuscript with recombinant reagents that were instrumental in setting up the workflow and are hopeful to see this new technique adapted in many chromatin and mass spectrometry laboratories."
Congratulations to all involved in the lab's latest Nature Communications publication. Read the full article here