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L3MBTL1 recognition of mono- and dimethylated histones

Nature Structural & Molecular Biology volume 14, pages 1229–1230 (2007)Cite this article

An Erratum to this article was published on 01 January 2008

This article has been updated

Abstract

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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Figure 1: The second MBT repeat of L3MBTL1 binds H4K20me2.
Figure 2: Comparison of lysine-binding pockets in L3MBTL1 and 53BP1.

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Accession codes

Primary accessions

Protein Data Bank

Change history

  • 18 December 2007

    In the version of this article initially published, the "Accession codes" section was missing. The section should read: Accession codes. Protein Data Bank: Coordinates and structure factors have codes 2PQW, 2RJE and 2RJF (L3MBTL1–H4K20me2 complexes), 2RJD (L3MBTL1 apo-structure) and 2RJC (L3MBTL1–MES complex). The error has been corrected in the HTML and PDF versions of the article.

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Acknowledgements

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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Authors and Affiliations

  1. Structural Genomics Consortium, University of Toronto, 100 College Street, Toronto, M5G 1L5, Ontario, Canada

    Jinrong Min, Abdellah Allali-Hassani, Chao Qi, Hui Ouyang, Yongsong Liu, Farrell MacKenzie, Masoud Vedadi & Cheryl H Arrowsmith

  2. College of Life Science, Huazhong Normal University, 430079, Wuhan, P.R. China

    Jinrong Min & Chao Qi

  3. Ontario Cancer Institute and Department of Medical Biophysics, University of Toronto, 101 College Street, Toronto, M5G 1L7, Ontario, Canada

    Nataliya Nady & Cheryl H Arrowsmith

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  1. Jinrong Min
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Correspondence to Jinrong Min.

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Supplementary Figures 1–3, Supplementary Tables 1 and 2, Supplementary Methods (PDF 1838 kb)

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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

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