Structural highlights
Function
CBX1_HUMAN Component of heterochromatin. Recognizes and binds histone H3 tails methylated at 'Lys-9', leading to epigenetic repression. Interaction with lamin B receptor (LBR) can contribute to the association of the heterochromatin with the inner nuclear membrane.
Publication Abstract from PubMed
Protein-protein interactions mediated by methyllysine are ubiquitous in biological systems. Specific perturbation of such interactions has remained a challenging endeavor. Herein, we describe an allele-specific strategy toward an engineered protein-protein interface orthogonal to the human proteome. We develop a methyltransferase (writer) variant that installs aryllysine moiety on histones that can only be recognized by an engineered chromodomain (reader). We establish biochemical integrity of the engineered interface, provide structural evidence for orthogonality and validate its applicability to identify transcriptional regulators. Our approach provides an unprecedented strategy for specific manipulation of the methyllysine interactome.
Engineering Methyllysine Writers and Readers for Allele-Specific Regulation of Protein-Protein Interactions.,Arora S, Horne WS, Islam K J Am Chem Soc. 2019 Oct 2;141(39):15466-15470. doi: 10.1021/jacs.9b05725. Epub, 2019 Sep 20. PMID:31518125[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Arora S, Horne WS, Islam K. Engineering Methyllysine Writers and Readers for Allele-Specific Regulation of Protein-Protein Interactions. J Am Chem Soc. 2019 Oct 2;141(39):15466-15470. doi: 10.1021/jacs.9b05725. Epub, 2019 Sep 20. PMID:31518125 doi:http://dx.doi.org/10.1021/jacs.9b05725
