The structural basis of modified nucleosome recognition by 53BP1

Marcus D. Wilson, Samir Benlekbir, Amélie Fradet-Turcotte, Alana Sherker, Jean-Philippe Julien, Andrea McEwan, Sylvie M. Noordermeer, Frank Sicheri (), John L. Rubinstein () and Daniel Durocher ()
Additional contact information
Marcus D. Wilson: The Lunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital, 600 University Avenue
Samir Benlekbir: Molecular Structure and Function Program, The Hospital for Sick Children Research Institute
Amélie Fradet-Turcotte: The Lunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital, 600 University Avenue
Alana Sherker: The Lunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital, 600 University Avenue
Jean-Philippe Julien: Molecular Structure and Function Program, The Hospital for Sick Children Research Institute
Andrea McEwan: The Lunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital, 600 University Avenue
Sylvie M. Noordermeer: The Lunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital, 600 University Avenue
Frank Sicheri: The Lunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital, 600 University Avenue
John L. Rubinstein: Molecular Structure and Function Program, The Hospital for Sick Children Research Institute
Daniel Durocher: The Lunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital, 600 University Avenue

Nature, 2016, vol. 536, issue 7614, 100-103

Abstract: A cryo-electron microscopy structure of the DNA damage repair protein 53BP1 bound to a nucleosome illuminates the way 53BP1 recognizes two types of histone modifications (a methyl group and a ubiquitin moiety), and provides insight into the highly specified recognition and recruitment of 53BP1 to modified chromatin.

Date: 2016
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DOI: 10.1038/nature18951

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