36 research outputs found

    Dynamic protein methylation in chromatin biology

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    Post-translational modification of chromatin is emerging as an increasingly important regulator of chromosomal processes. In particular, histone lysine and arginine methylation play important roles in regulating transcription, maintaining genomic integrity, and contributing to epigenetic memory. Recently, the use of new approaches to analyse histone methylation, the generation of genetic model systems, and the ability to interrogate genome wide histone modification profiles has aided in defining how histone methylation contributes to these processes. Here we focus on the recent advances in our understanding of the histone methylation system and examine how dynamic histone methylation contributes to normal cellular function in mammals

    Tudor Domains as Methyl-Lysine and Methyl-Arginine Readers

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    Solution structure of 53BP1 tandem Tudor domains in complex with a p53K370me2 peptide

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    Structure of 53BP1 tandem Tudor domains in complex with small molecule UNC2991

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    Solution NMR structure of PHF20 PHD domain in complex with a histone H3K4me2 peptide

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    X-ray structure of human REV7 in complex with Shieldin3 (residues 41-74)

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    X-ray structure of SPOP MATH domain (D140G)

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    Structure of human TIRR

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    X-ray structure of SPOP MATH domain (S119D) in complex with a 53BP1 peptide

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    Structure of SPOP MATH domain in complex with a Geminin peptide

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