Structural Basis for the Methylation State-Specific Recognition of Histone H4-K20 by 53BP1 and Crb2 in DNA Repair
作者： Maria Victoria Botuyan , Joseph Lee , Irene M. Ward , Ja-Eun Kim , James R. Thompson
DOI: 10.1016/J.CELL.2006.10.043
关键词:
摘要: Histone lysine methylation has been linked to the recruitment of mammalian DNA repair factor 53BP1 and putative fission yeast homolog Crb2 double-strand breaks (DSBs), but how histone recognition is achieved not established. Here we demonstrate that this link occurs through direct binding H4. Using X-ray crystallography nuclear magnetic resonance (NMR) spectroscopy, show that, despite low amino acid sequence conservation, both contain tandem tudor domains interact with H4 specifically dimethylated at Lys20 (H4-K20me2). The structure 53BP1/H4-K20me2 complex uncovers a unique five-residue cage, remarkably conserved in Crb2, best accommodates dimethyllysine excludes trimethyllysine, thus explaining state-specific H4-K20. This study reveals an evolutionarily molecular mechanism targeting proteins DSBs by H4-K20me2.
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