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Structural Plasticity of Methyllysine Recognition by the Tandem Tudor Domain of 53BP1

Tong, Qiong, Cui, Gaofeng, Botuyan, Maria Victoria, Rothbart, Scott B., Hayashi, Ryo, Musselman, Catherine A., Singh, Namit, Appella, Ettore, Strahl, Brian D., Mer, Georges, Kutateladze, Tatiana G.·2015·Structure
DOI 10.1016/j.str.2014.11.013
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Research works printed but not linked: 44

  1. Botuyan, 2006, Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair, Cell, 127, 1361, 10.1016/j.cell.2006.10.043 · DOI · Paper page
  2. Carr, 2014, Lysine methylation-dependent binding of 53BP1 to the pRb tumor suppressor, Proc. Natl. Acad. Sci. USA, 111, 11341, 10.1073/pnas.1403737111 · DOI
  3. Case, 2005, The Amber biomolecular simulation programs, J. Comput. Chem., 26, 1668, 10.1002/jcc.20290 · DOI · Paper page
  4. Charier, 2004, The Tudor tandem of 53BP1: a new structural motif involved in DNA and RG-rich peptide binding, Structure, 12, 1551, 10.1016/j.str.2004.06.014 · DOI
  5. Chuikov, 2004, Regulation of p53 activity through lysine methylation, Nature, 432, 353, 10.1038/nature03117 · DOI · Paper page
  6. Cornilescu, 1999, Protein backbone angle restraints from searching a database for chemical shift and sequence homology, J. Biomol. NMR, 13, 289, 10.1023/A:1008392405740 · DOI · Paper page
  7. Cui, 2009, Preparation of recombinant peptides with site- and degree-specific lysine (13)C-methylation, Biochemistry, 48, 3798, 10.1021/bi900348z · DOI
  8. Cui, 2012, PHF20 is an effector protein of p53 double lysine methylation that stabilizes and activates p53, Nat. Struct. Mol. Biol., 19, 916, 10.1038/nsmb.2353 · DOI
  9. Dai, 2010, p53 post-translational modification: deregulated in tumorigenesis, Trends Mol. Med., 16, 528, 10.1016/j.molmed.2010.09.002 · DOI · Paper page
  10. Delaglio, 1995, NMRPipe: a multidimensional spectral processing system based on UNIX pipes, J. Biomol. NMR, 6, 277, 10.1007/BF00197809 · DOI · Paper page
  11. Duggan, 2001, SANE (Structure Assisted NOE Evaluation): an automated model-based approach for NOE assignment, J. Biomol. NMR, 19, 321, 10.1023/A:1011227824104 · DOI
  12. Fernandez-Capetillo, 2002, DNA damage-induced G2-M checkpoint activation by histone H2AX and 53BP1, Nat. Cell Biol., 4, 993, 10.1038/ncb884 · DOI · Paper page
  13. Fnu, 2011, Methylation of histone H3 lysine 36 enhances DNA repair by nonhomologous end-joining, Proc. Natl. Acad. Sci. USA, 108, 540, 10.1073/pnas.1013571108 · DOI · Paper page
  14. Gatchalian, 2013, Dido3 PHD modulates cell differentiation and division, Cell Rep., 4, 148, 10.1016/j.celrep.2013.06.014 · DOI
  15. Güntert, 2004, Automated NMR structure calculation with CYANA, Methods Mol. Biol., 278, 353
  16. Huang, 2008, The emerging field of dynamic lysine methylation of non-histone proteins, Curr. Opin. Genet. Dev., 18, 152, 10.1016/j.gde.2008.01.012 · DOI · Paper page
  17. Huang, 2006, Repression of p53 activity by Smyd2-mediated methylation, Nature, 444, 629, 10.1038/nature05287 · DOI · Paper page
  18. Huang, 2007, p53 is regulated by the lysine demethylase LSD1, Nature, 449, 105, 10.1038/nature06092 · DOI · Paper page
  19. Huang, 2010, G9a and Glp methylate lysine 373 in the tumor suppressor p53, J. Biol. Chem., 285, 9636, 10.1074/jbc.M109.062588 · DOI · Paper page
  20. Jha, 2014, An RNA polymerase II-coupled function for histone H3K36 methylation in checkpoint activation and DSB repair, Nat. Commun., 5, 3965, 10.1038/ncomms4965 · DOI
  21. Johnson, 1994, NMR View: a computer program for visualization and analysis of NMR data, J. Biomol. NMR, 4, 603, 10.1007/BF00404272 · DOI · Paper page
  22. Kachirskaia, 2008, Role for 53BP1 Tudor domain recognition of p53 dimethylated at lysine 382 in DNA damage signaling, J. Biol. Chem., 283, 34660, 10.1074/jbc.M806020200 · DOI
  23. Kim, 2006, Tudor, MBT and chromo domains gauge the degree of lysine methylation, EMBO Rep., 7, 397, 10.1038/sj.embor.7400625 · DOI · Paper page
  24. Lee, 2008, Distinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor, Nat. Struct. Mol. Biol., 15, 109, 10.1038/nsmb1326 · DOI · Paper page
  25. Mer, 2000, Structural basis for the recognition of DNA repair proteins UNG2, XPA, and RAD52 by replication factor RPA, Cell, 103, 449, 10.1016/S0092-8674(00)00136-7 · DOI · Paper page
  26. Mujtaba, 2004, Structural mechanism of the bromodomain of the coactivator CBP in p53 transcriptional activation, Mol. Cell, 13, 251, 10.1016/S1097-2765(03)00528-8 · DOI · Paper page
  27. Muller, 2013, p53 mutations in cancer, Nat. Cell Biol., 15, 2, 10.1038/ncb2641 · DOI · Paper page
  28. Musselman, 2009, Binding of the CHD4 PHD2 finger to histone H3 is modulated by covalent modifications, Biochem. J., 423, 179, 10.1042/BJ20090870 · DOI
  29. Musselman, 2012, Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1, Nat. Struct. Mol. Biol., 19, 1266, 10.1038/nsmb.2435 · DOI · Paper page
  30. Musselman, 2012, Bivalent recognition of nucleosomes by the tandem PHD fingers of the CHD4 ATPase is required for CHD4-mediated repression, Proc. Natl. Acad. Sci. USA, 109, 787, 10.1073/pnas.1113655109 · DOI
  31. Pai, 2014, A histone H3K36 chromatin switch coordinates DNA double-strand break repair pathway choice, Nat. Commun., 5, 4091, 10.1038/ncomms5091 · DOI
  32. Panier, 2014, Double-strand break repair: 53BP1 comes into focus, Nat. Rev. Mol. Cell Biol., 15, 7, 10.1038/nrm3719 · DOI · Paper page
  33. Rappold, 2001, Tumor suppressor p53 binding protein 1 (53BP1) is involved in DNA damage-signaling pathways, J. Cell Biol., 153, 613, 10.1083/jcb.153.3.613 · DOI · Paper page
  34. Roy, 2010, Structural insight into p53 recognition by the 53BP1 tandem Tudor domain, J. Mol. Biol., 398, 489, 10.1016/j.jmb.2010.03.024 · DOI
  35. Shi, 2007, Modulation of p53 function by SET8-mediated methylation at lysine 382, Mol. Cell, 27, 636, 10.1016/j.molcel.2007.07.012 · DOI · Paper page
  36. Strahl, 2000, The language of covalent histone modifications, Nature, 403, 41, 10.1038/47412 · DOI · Paper page
  37. Tsui, 2000, Theory and applications of the generalized Born solvation model in macromolecular simulations, Biopolymers, 56, 275, 10.1002/1097-0282(2000)56:4<275::AID-BIP10024>3.0.CO;2-E · DOI · Paper page
  38. Vousden, 2007, p53 in health and disease, Nat. Rev. Mol. Cell Biol., 8, 275, 10.1038/nrm2147 · DOI · Paper page
  39. Ward, 2006, The tandem BRCT domain of 53BP1 is not required for its repair function, J. Biol. Chem., 281, 38472, 10.1074/jbc.M607577200 · DOI
  40. West, 2010, The MBT repeats of L3MBTL1 link SET8-mediated p53 methylation at lysine 382 to target gene repression, J. Biol. Chem., 285, 37725, 10.1074/jbc.M110.139527 · DOI
  41. Wishart, 1994, The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data, J. Biomol. NMR, 4, 171, 10.1007/BF00175245 · DOI · Paper page
  42. Zgheib, 2009, An oligomerized 53BP1 tudor domain suffices for recognition of DNA double-strand breaks, Mol. Cell Biol., 29, 1050, 10.1128/MCB.01011-08 · DOI
  43. Zhang, 2012, Lysine methylation: beyond histones, Acta Biochim. Biophys. Sin. (Shanghai), 44, 14, 10.1093/abbs/gmr100 · DOI · Paper page
  44. Zwahlen, 1997, Methods of measurements of intermolecular NOEs by multinuclear NMR spectroscopy: application to a bacteriophage N-peptide/box B RNA complex, J. Am. Chem. Soc., 119, 6711, 10.1021/ja970224q · DOI · Paper page

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Metadata

Authors
Tong, Q., Cui, G., Botuyan, M. V., Rothbart, S. B., Hayashi, R., Musselman, C. A., Singh, N., Appella, E., Strahl, B. D., Mer, G., & Kutateladze, T. G.
Venue
Structure
Publisher
Elsevier BV
Published
2015-02
Volume
23
Issue
2
Pages
312-321
ISSN
0969-2126
DOI
10.1016/j.str.2014.11.013
Cited by
37
References
7
Language
en
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CoChat. (2026). Citation check: Structural Plasticity of Methyllysine Recognition by the Tandem Tudor Domain of 53BP1. https://app.cochat.ai/papers/10.1016/j.str.2014.11.013
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Tong, Q., Cui, G., Botuyan, M. V., Rothbart, S. B., Hayashi, R., Musselman, C. A., Singh, N., Appella, E., Strahl, B. D., Mer, G., & Kutateladze, T. G. (2015). Structural Plasticity of Methyllysine Recognition by the Tandem Tudor Domain of 53BP1. Structure. https://doi.org/10.1016/j.str.2014.11.013

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