Crystal structures of the L3MBTL1 MBT repeats in complex with histone H4 peptides dimethylated on Lys20 (H4K20me2) show that only the second of the three MBT repeats can bind mono- and dimethylated histone peptides. Its binding pocket has similarities to that of 53BP1 and is able to recognize the degree of histone lysine methylation. An unexpected mode of peptide-mediated dimerization suggests a possible mechanism for chromatin compaction by L3MBTL1.
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We thank A. Edwards for critically reading and discussing the manuscript, and M. Schapira, I. Kozieradzki, A. Dong, G. Senisterra, G. Wasney, P. Loppnau and L. Crombet for technical assistance and advice. This research was supported by the Structural Genomics Consortium, a registered charity (number 1097737) that receives funds from the Canadian Institutes for Health Research, the Canadian Foundation for Innovation, Genome Canada through the Ontario Genomics Institute, GlaxoSmithKline, Karolinska Institutet, the Knut and Alice Wallenberg Foundation, the Ontario Innovation Trust, the Ontario Ministry for Research and Innovation, Merck & Co., the Novartis Research Foundation, the Swedish Agency for Innovation Systems, the Swedish Foundation for Strategic Research and the Wellcome Trust. Additional support was provided by the National Science Foundation of China (30670429 to J.M. and C.Q.) and the National Cancer Institute of Canada with funds from the Canadian Cancer Society (C.H.A. and N.N.).
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Min, J., Allali-Hassani, A., Nady, N. et al. L3MBTL1 recognition of mono- and dimethylated histones. Nat Struct Mol Biol 14, 1229–1230 (2007). https://doi.org/10.1038/nsmb1340