Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1.
作者： Qiong Tong , Gaofeng Cui , Maria Victoria Botuyan , Scott B. Rothbart , Ryo Hayashi
DOI: 10.1016/J.STR.2014.11.013
关键词: Peptide sequence 、 Tudor domain 、 DNA methylation 、 Histone 、 Methyllysine 、 Peptide 、 Protein structure 、 Computational biology 、 Function (biology) 、 Biology 、 Biochemistry
摘要: p53 is dynamically regulated through various posttranslational modifications (PTMs), which differentially modulate its function and stability. The dimethylated marks p53K370me2 p53K382me2 are associated with activation or stabilization both recognized by the tandem Tudor domain (TTD) of 53BP1, a cofactor. Here we detail molecular mechanisms for recognition 53BP1. solution structures TTD in complex peptides show remarkable plasticity 53BP1 accommodating these diverse dimethyllysine-containing sequences. We demonstrate that dimeric TTDs capable interacting two PTMs on single p53K370me2K382me2 peptide, greatly strengthening 53BP1-p53 interaction. Analysis binding affinities toward methylated histones reveals strong preference p53K382me2, H4K20me2, H3K36me2 suggests possible role multivalent contacts targeting to accumulation at sites DNA damage.
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Brendan M. Duggan, Glen B. Legge, H. Jane Dyson, Peter E. Wright, SANE (Structure Assisted NOE Evaluation): an automated model-based approach for NOE assignment. Journal of Biomolecular NMR. ,vol. 19, pp. 321- 329 ,(2001) , 10.1023/A:1011227824104
Peter Güntert, Automated NMR structure calculation with CYANA. Methods of Molecular Biology. ,vol. 278, pp. 353- 378 ,(2004) , 10.1385/1-59259-809-9:353
Gabriel Cornilescu, Frank Delaglio, Ad Bax, Protein backbone angle restraints from searching a database for chemical shift and sequence homology Journal of Biomolecular NMR. ,vol. 13, pp. 289- 302 ,(1999) , 10.1023/A:1008392405740
Joseph Lee, James R Thompson, Maria Victoria Botuyan, Georges Mer, Distinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor Nature Structural & Molecular Biology. ,vol. 15, pp. 109- 111 ,(2008) , 10.1038/NSMB1326
Jing Huang, Shelley L Berger, The emerging field of dynamic lysine methylation of non-histone proteins Current Opinion in Genetics & Development. ,vol. 18, pp. 152- 158 ,(2008) , 10.1016/J.GDE.2008.01.012
Arnold J. Levine, Moshe Oren, The first 30 years of p53: growing ever more complex Nature Reviews Cancer. ,vol. 9, pp. 749- 758 ,(2009) , 10.1038/NRC2723
Ran Brosh, Varda Rotter, When mutants gain new powers: news from the mutant p53 field Nature Reviews Cancer. ,vol. 9, pp. 701- 713 ,(2009) , 10.1038/NRC2693
Irene Ward, Ja-Eun Kim, Kay Minn, Claudia C. Chini, Georges Mer, Junjie Chen, The Tandem BRCT Domain of 53BP1 Is Not Required for Its Repair Function Journal of Biological Chemistry. ,vol. 281, pp. 38472- 38477 ,(2006) , 10.1074/JBC.M607577200
Zengqiang Yuan, Maria Victoria Botuyan, Mark T Bedford, Jin Q Cheng, Georges Mer, Gaofeng Cui, Sungman Park, Aimee I Badeaux, Donghwa Kim, Joseph Lee, James R Thompson, Fei Yan, Satoshi Kaneko, PHF20 is an effector protein of p53 double lysine methylation that stabilizes and activates p53. Nature Structural & Molecular Biology. ,vol. 19, pp. 916- 924 ,(2012) , 10.1038/NSMB.2353
S. M. Carr, S. Munro, L.-P. Zalmas, O. Fedorov, C. Johansson, T. Krojer, C. A. Sagum, M. T. Bedford, U. Oppermann, N. B. La Thangue, Lysine methylation-dependent binding of 53BP1 to the pRb tumor suppressor. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 111, pp. 11341- 11346 ,(2014) , 10.1073/PNAS.1403737111