Mechanisms of BRCA1–BARD1 nucleosome recognition and ubiquitylation

The BRCA1–BARD1 tumour suppressor is an E3 ubiquitin ligase necessary for the repair of DNA double-strand breaks by homologous recombination 1 – 10 . The BRCA1–BARD1 complex localizes to damaged chromatin after DNA replication and catalyses the ubiquitylation of histone H2A and other cellular target...

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Published inNature (London) Vol. 596; no. 7872; pp. 438 - 443
Main Authors Hu, Qi, Botuyan, Maria Victoria, Zhao, Debiao, Cui, Gaofeng, Mer, Elie, Mer, Georges
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 19.08.2021
Nature Publishing Group
Subjects
101/28
101/6
631/337/100/1701
631/337/1427/2122
631/337/458/582
631/535/1258/1259
631/535/878/1263
82
82/16
82/6
82/80
82/83
Amino acids
Ankyrins
BRCA1 protein
BRCA1 Protein - metabolism
Breast cancer
C-Terminus
Cancer
Chromatin
Crosstalk
Cryoelectron Microscopy
Damage localization
Deoxyribonucleic acid
DNA
DNA biosynthesis
DNA Repair
Domains
Electron microscopy
Enzymes
Flexibility
Genetic aspects
Histone H2A
Histones
Histones - chemistry
Histones - metabolism
Homologous Recombination
Homology
Humanities and Social Sciences
Humans
Microscopy
Models, Molecular
multidisciplinary
Mutation
Neoplasms - genetics
NMR
Nuclear magnetic resonance
Nucleosomes
Nucleosomes - chemistry
Nucleosomes - genetics
Nucleosomes - metabolism
Nucleosomes - ultrastructure
Physiological aspects
Protein Domains
Proteins
Recruitment
Repair
Science
Science (multidisciplinary)
Spectrum analysis
Target recognition
Tumor suppressor genes
Tumor Suppressor p53-Binding Protein 1 - antagonists & inhibitors
Tumor Suppressor p53-Binding Protein 1 - metabolism
Tumor Suppressor Proteins - chemistry
Tumor Suppressor Proteins - genetics
Tumor Suppressor Proteins - metabolism
Tumor Suppressor Proteins - ultrastructure
Tumors
Ubiquitin
Ubiquitin - metabolism
Ubiquitin-conjugating enzyme
Ubiquitin-Conjugating Enzymes - chemistry
Ubiquitin-Conjugating Enzymes - metabolism
Ubiquitin-Conjugating Enzymes - ultrastructure
Ubiquitin-protein ligase
Ubiquitin-Protein Ligases - chemistry
Ubiquitin-Protein Ligases - genetics
Ubiquitin-Protein Ligases - metabolism
Ubiquitin-Protein Ligases - ultrastructure
Ubiquitination
United States
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Abstract The BRCA1–BARD1 tumour suppressor is an E3 ubiquitin ligase necessary for the repair of DNA double-strand breaks by homologous recombination 1 – 10 . The BRCA1–BARD1 complex localizes to damaged chromatin after DNA replication and catalyses the ubiquitylation of histone H2A and other cellular targets 11 – 14 . The molecular bases for the recruitment to double-strand breaks and target recognition of BRCA1–BARD1 remain unknown. Here we use cryo-electron microscopy to show that the ankyrin repeat and tandem BRCT domains in BARD1 adopt a compact fold and bind to nucleosomal histones, DNA and monoubiquitin attached to H2A amino-terminal K13 or K15, two signals known to be specific for double-strand breaks 15 , 16 . We further show that RING domains 17 in BRCA1–BARD1 orient an E2 ubiquitin-conjugating enzyme atop the nucleosome in a dynamic conformation, primed for ubiquitin transfer to the flexible carboxy-terminal tails of H2A and variant H2AX. Our work reveals a regulatory crosstalk in which recognition of monoubiquitin by BRCA1–BARD1 at the N terminus of H2A blocks the formation of polyubiquitin chains and cooperatively promotes ubiquitylation at the C terminus of H2A. These findings elucidate the mechanisms of BRCA1–BARD1 chromatin recruitment and ubiquitylation specificity, highlight key functions of BARD1 in both processes and explain how BRCA1–BARD1 promotes homologous recombination by opposing the DNA repair protein 53BP1 in post-replicative chromatin 18 – 22 . These data provide a structural framework to evaluate BARD1 variants and help to identify mutations that drive the development of cancer. The authors elucidate the mechanisms for the ubiquitylation specificity and recruitment of the ubiquitin ligase complex BRCA1–BARD1 to damaged DNA within chromatin to facilitate homologous recombination.
AbstractList The BRCA1-BARD1 tumour suppressor is an E3 ubiquitin ligase necessary for the repair of DNA double-strand breaks by homologous recombination.sup.1-10. The BRCA1-BARD1 complex localizes to damaged chromatin after DNA replication and catalyses the ubiquitylation of histone H2A and other cellular targets.sup.11-14. The molecular bases for the recruitment to double-strand breaks and target recognition of BRCA1-BARD1 remain unknown. Here we use cryo-electron microscopy to show that the ankyrin repeat and tandem BRCT domains in BARD1 adopt a compact fold and bind to nucleosomal histones, DNA and monoubiquitin attached to H2A amino-terminal K13 or K15, two signals known to be specific for double-strand breaks.sup.15,16. We further show that RING domains.sup.17 in BRCA1-BARD1 orient an E2 ubiquitin-conjugating enzyme atop the nucleosome in a dynamic conformation, primed for ubiquitin transfer to the flexible carboxy-terminal tails of H2A and variant H2AX. Our work reveals a regulatory crosstalk in which recognition of monoubiquitin by BRCA1-BARD1 at the N terminus of H2A blocks the formation of polyubiquitin chains and cooperatively promotes ubiquitylation at the C terminus of H2A. These findings elucidate the mechanisms of BRCA1-BARD1 chromatin recruitment and ubiquitylation specificity, highlight key functions of BARD1 in both processes and explain how BRCA1-BARD1 promotes homologous recombination by opposing the DNA repair protein 53BP1 in post-replicative chromatin.sup.18-22. These data provide a structural framework to evaluate BARD1 variants and help to identify mutations that drive the development of cancer.
The BRCA1-BARD1 tumour suppressor is an E3 ubiquitin ligase necessary for the repair of DNA double-strand breaks by homologous recombination1-10. The BRCA1-BARD1 complex localizes to damaged chromatin after DNA replication and catalyses the ubiquitylation of histone H2A and other cellular targets11-14. The molecular bases for the recruitment to double-strand breaks and target recognition of BRCA1-BARD1 remain unknown. Here we use cryo-electron microscopy to show that the ankyrin repeat and tandem BRCT domains in BARD1 adopt a compact fold and bind to nucleosomal histones, DNA and monoubiquitin attached to H2A amino-terminal K13 or K15, two signals known to be specific for double-strand breaks15,16. We further show that RING domains17 in BRCA1-BARD1 orient an E2 ubiquitin-conjugating enzyme atop the nucleosome in a dynamic conformation, primed for ubiquitin transfer to the flexible carboxy-terminal tails of H2A and variant H2AX. Our work reveals a regulatory crosstalk in which recognition of monoubiquitin by BRCA1-BARD1 at the N terminus of H2A blocks the formation of polyubiquitin chains and cooperatively promotes ubiquitylation at the C terminus of H2A. These findings elucidate the mechanisms of BRCA1-BARD1 chromatin recruitment and ubiquitylation specificity, highlight key functions of BARD1 in both processes and explain how BRCA1-BARD1 promotes homologous recombination by opposing the DNA repair protein 53BP1 in post-replicative chromatin18-22. These data provide a structural framework to evaluate BARD1 variants and help to identify mutations that drive the development of cancer.The BRCA1-BARD1 tumour suppressor is an E3 ubiquitin ligase necessary for the repair of DNA double-strand breaks by homologous recombination1-10. The BRCA1-BARD1 complex localizes to damaged chromatin after DNA replication and catalyses the ubiquitylation of histone H2A and other cellular targets11-14. The molecular bases for the recruitment to double-strand breaks and target recognition of BRCA1-BARD1 remain unknown. Here we use cryo-electron microscopy to show that the ankyrin repeat and tandem BRCT domains in BARD1 adopt a compact fold and bind to nucleosomal histones, DNA and monoubiquitin attached to H2A amino-terminal K13 or K15, two signals known to be specific for double-strand breaks15,16. We further show that RING domains17 in BRCA1-BARD1 orient an E2 ubiquitin-conjugating enzyme atop the nucleosome in a dynamic conformation, primed for ubiquitin transfer to the flexible carboxy-terminal tails of H2A and variant H2AX. Our work reveals a regulatory crosstalk in which recognition of monoubiquitin by BRCA1-BARD1 at the N terminus of H2A blocks the formation of polyubiquitin chains and cooperatively promotes ubiquitylation at the C terminus of H2A. These findings elucidate the mechanisms of BRCA1-BARD1 chromatin recruitment and ubiquitylation specificity, highlight key functions of BARD1 in both processes and explain how BRCA1-BARD1 promotes homologous recombination by opposing the DNA repair protein 53BP1 in post-replicative chromatin18-22. These data provide a structural framework to evaluate BARD1 variants and help to identify mutations that drive the development of cancer.
The BRCA1-BARD1 tumour suppressor is an E3 ubiquitin ligase necessary for the repair of DNA double-strand breaks by homologous recombination.sup.1-10. The BRCA1-BARD1 complex localizes to damaged chromatin after DNA replication and catalyses the ubiquitylation of histone H2A and other cellular targets.sup.11-14. The molecular bases for the recruitment to double-strand breaks and target recognition of BRCA1-BARD1 remain unknown. Here we use cryo-electron microscopy to show that the ankyrin repeat and tandem BRCT domains in BARD1 adopt a compact fold and bind to nucleosomal histones, DNA and monoubiquitin attached to H2A amino-terminal K13 or K15, two signals known to be specific for double-strand breaks.sup.15,16. We further show that RING domains.sup.17 in BRCA1-BARD1 orient an E2 ubiquitin-conjugating enzyme atop the nucleosome in a dynamic conformation, primed for ubiquitin transfer to the flexible carboxy-terminal tails of H2A and variant H2AX. Our work reveals a regulatory crosstalk in which recognition of monoubiquitin by BRCA1-BARD1 at the N terminus of H2A blocks the formation of polyubiquitin chains and cooperatively promotes ubiquitylation at the C terminus of H2A. These findings elucidate the mechanisms of BRCA1-BARD1 chromatin recruitment and ubiquitylation specificity, highlight key functions of BARD1 in both processes and explain how BRCA1-BARD1 promotes homologous recombination by opposing the DNA repair protein 53BP1 in post-replicative chromatin.sup.18-22. These data provide a structural framework to evaluate BARD1 variants and help to identify mutations that drive the development of cancer. The authors elucidate the mechanisms for the ubiquitylation specificity and recruitment of the ubiquitin ligase complex BRCA1-BARD1 to damaged DNA within chromatin to facilitate homologous recombination.
The BRCA1–BARD1 tumour suppressor is an E3 ubiquitin ligase necessary for the repair of DNA double-strand breaks by homologous recombination 1 – 10 . The BRCA1–BARD1 complex localizes to damaged chromatin after DNA replication and catalyses the ubiquitylation of histone H2A and other cellular targets 11 – 14 . The molecular bases for the recruitment to double-strand breaks and target recognition of BRCA1–BARD1 remain unknown. Here we use cryo-electron microscopy to show that the ankyrin repeat and tandem BRCT domains in BARD1 adopt a compact fold and bind to nucleosomal histones, DNA and monoubiquitin attached to H2A amino-terminal K13 or K15, two signals known to be specific for double-strand breaks 15 , 16 . We further show that RING domains 17 in BRCA1–BARD1 orient an E2 ubiquitin-conjugating enzyme atop the nucleosome in a dynamic conformation, primed for ubiquitin transfer to the flexible carboxy-terminal tails of H2A and variant H2AX. Our work reveals a regulatory crosstalk in which recognition of monoubiquitin by BRCA1–BARD1 at the N terminus of H2A blocks the formation of polyubiquitin chains and cooperatively promotes ubiquitylation at the C terminus of H2A. These findings elucidate the mechanisms of BRCA1–BARD1 chromatin recruitment and ubiquitylation specificity, highlight key functions of BARD1 in both processes and explain how BRCA1–BARD1 promotes homologous recombination by opposing the DNA repair protein 53BP1 in post-replicative chromatin 18 – 22 . These data provide a structural framework to evaluate BARD1 variants and help to identify mutations that drive the development of cancer. The authors elucidate the mechanisms for the ubiquitylation specificity and recruitment of the ubiquitin ligase complex BRCA1–BARD1 to damaged DNA within chromatin to facilitate homologous recombination.
The BRCA1–BARD1 tumour suppressor is an E3 ubiquitin ligase necessary for the repair of DNA double-strand breaks by homologous recombination 1 – 10 . The BRCA1–BARD1 complex localizes to damaged chromatin after DNA replication and catalyses the ubiquitylation of histone H2A and other cellular targets 11 – 14 . The molecular bases for the recruitment to double-strand breaks and target recognition of BRCA1–BARD1 remain unknown. Here we use cryo-electron microscopy to show that the ankyrin repeat and tandem BRCT domains in BARD1 adopt a compact fold and bind to nucleosomal histones, DNA and monoubiquitin attached to H2A amino-terminal K13 or K15, two signals known to be specific for double-strand breaks 15 , 16 . We further show that RING domains 17 in BRCA1–BARD1 orient an E2 ubiquitin-conjugating enzyme atop the nucleosome in a dynamic conformation, primed for ubiquitin transfer to the flexible carboxy-terminal tails of H2A and variant H2AX. Our work reveals a regulatory crosstalk in which recognition of monoubiquitin by BRCA1–BARD1 at the N terminus of H2A blocks the formation of polyubiquitin chains and cooperatively promotes ubiquitylation at the C terminus of H2A. These findings elucidate the mechanisms of BRCA1–BARD1 chromatin recruitment and ubiquitylation specificity, highlight key functions of BARD1 in both processes and explain how BRCA1-BARD1 promotes homologous recombination by opposing the DNA repair protein 53BP1 in post-replicative chromatin 18 – 22 . These data provide a structural framework to evaluate BARD1 variants and help to identify mutations that drive the development of cancer.
The BRCA1-BARD1 tumour suppressor is an E3 ubiquitin ligase necessary for the repair ofDNA double-strand breaks by homologous recombination. The BRCA1-BARD1 complex localizes to damaged chromatin after DNA replication and catalyses the ubiquitylation of histone H2A and other cellular targets. The molecular bases for the recruitment to double-strand breaks and target recognition of BRCA1-BARD1 remain unknown. Here we use cryo-electron microscopy to show that the ankyrin repeat and tandem BRCT domains in BARD1 adopt a compact fold and bind to nucleosomal histones, DNA and monoubiquitin attached to H2A amino-terminal K13 or K15, two signals known to be specific for double-strand breaks. We further show that RING domains in BRCA1-BARD1 orient an E2 ubiquitin-conjugating enzyme atop the nucleosome in a dynamic conformation, primed for ubiquitin transfer to the flexible carboxy-terminal tails of H2A and variant H2AX. Our work reveals a regulatory crosstalk in which recognition of monoubiquitin by BRCA1-BARD1 at the N terminus of H2A blocks the formation of polyubiquitin chains and cooperatively promotes ubiquitylation at the C terminus of H2A. These findings elucidate the mechanisms of BRCA1-BARD1 chromatin recruitment and ubiquitylation specificity, highlight key functions ofBARD1 in both processes and explain how BRCA1-BARD1 promotes homologous recombination by opposing the DNA repair protein 53BP1 in post-replicative chromatin. These data provide a structural framework to evaluate BARD1 variants and help to identify mutations that drive the development of cancer.
The BRCA1-BARD1 tumour suppressor is an E3 ubiquitin ligase necessary for the repair of DNA double-strand breaks by homologous recombination . The BRCA1-BARD1 complex localizes to damaged chromatin after DNA replication and catalyses the ubiquitylation of histone H2A and other cellular targets . The molecular bases for the recruitment to double-strand breaks and target recognition of BRCA1-BARD1 remain unknown. Here we use cryo-electron microscopy to show that the ankyrin repeat and tandem BRCT domains in BARD1 adopt a compact fold and bind to nucleosomal histones, DNA and monoubiquitin attached to H2A amino-terminal K13 or K15, two signals known to be specific for double-strand breaks . We further show that RING domains in BRCA1-BARD1 orient an E2 ubiquitin-conjugating enzyme atop the nucleosome in a dynamic conformation, primed for ubiquitin transfer to the flexible carboxy-terminal tails of H2A and variant H2AX. Our work reveals a regulatory crosstalk in which recognition of monoubiquitin by BRCA1-BARD1 at the N terminus of H2A blocks the formation of polyubiquitin chains and cooperatively promotes ubiquitylation at the C terminus of H2A. These findings elucidate the mechanisms of BRCA1-BARD1 chromatin recruitment and ubiquitylation specificity, highlight key functions of BARD1 in both processes and explain how BRCA1-BARD1 promotes homologous recombination by opposing the DNA repair protein 53BP1 in post-replicative chromatin . These data provide a structural framework to evaluate BARD1 variants and help to identify mutations that drive the development of cancer.
Audience Academic
Author Zhao, Debiao
Botuyan, Maria Victoria
Cui, Gaofeng
Mer, Elie
Hu, Qi
Mer, Georges
AuthorAffiliation 1 Department of Biochemistry and Molecular Biology, Mayo Clinic, Rochester, MN, USA
2 Department of Cancer Biology, Mayo Clinic, Rochester, MN, USA
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/34321665$$D View this record in MEDLINE/PubMed
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Cites_doi 10.1016/S0092-8674(00)81847-4
10.1016/j.ccr.2013.03.025
10.1038/s41594-020-00556-4
10.7554/eLife.36861
10.1038/38444
10.1126/sciadv.1701386
10.1021/bi025571d
10.1038/nsmb.1831
10.4161/cc.20919
10.1126/science.1139516
10.1038/s41586-019-1259-3
10.1007/s10858-005-4425-x
10.1002/jcc.20084
10.1074/jbc.C000881200
10.1038/s41556-018-0152-x
10.1073/pnas.111125998
10.1016/S0960-9822(00)00610-2
10.1016/j.celrep.2014.07.025
10.1107/S0907444909042073
10.1107/S2059798319011471
10.1016/j.cell.2006.10.043
10.1016/j.cell.2008.12.042
10.1038/nature13430
10.1074/jbc.M802333200
10.1038/emboj.2011.243
10.1126/science.7939630
10.1038/ng1294-399
10.1038/s41580-020-0218-z
10.1016/S1097-2765(00)80202-6
10.1074/jbc.C111.220715
10.1038/s41556-019-0282-9
10.1016/j.cell.2008.12.041
10.1038/nsmb.3236
10.1016/0010-4655(95)00042-E
10.1073/pnas.1715467115
10.1016/j.jsb.2012.09.006
10.1038/nature10861
10.1096/fj.201701413RRR
10.1126/science.1139621
10.1038/nsb1001-833
10.1126/science.1139476
10.1002/pro.3235
10.1016/j.molcel.2018.08.016
10.1016/j.ab.2011.06.034
10.1101/gad.2011011
10.1038/nmeth.4347
10.1038/nature18312
10.1089/adt.2005.3.613
10.1016/j.str.2010.04.017
10.1007/BF00197809
10.7554/eLife.42166
10.1016/j.molcel.2017.04.009
10.1016/S0076-6879(99)04003-3
10.1016/j.celrep.2017.05.016
10.1038/nature24060
10.1107/S0907444904019158
10.1093/emboj/cdf691
10.1016/j.jsb.2021.107702
10.1093/nar/gkx1153
10.1021/bi801115g
10.1093/bioinformatics/btu830
10.1016/j.cell.2010.03.012
10.1038/nmeth.4169
10.1016/j.cell.2012.08.005
10.1038/nsmb1148
10.1021/bi101303t
10.1074/jbc.M110.213728
10.1038/nmeth.4193
10.1038/nature18951
10.1038/nature09321
10.1038/nature12318
10.1126/science.1178994
10.1126/science.7545954
10.1038/ng1296-430
10.1126/science.2270482
10.1038/nature13890
10.1016/0022-2836(87)90679-6
10.1021/bi700323t
10.1242/jcs.105353
10.1101/2020.06.01.127951
ContentType Journal Article
Copyright The Author(s), under exclusive licence to Springer Nature Limited 2021. corrected publication 2021
2021. The Author(s), under exclusive licence to Springer Nature Limited.
COPYRIGHT 2021 Nature Publishing Group
Copyright Nature Publishing Group Aug 19, 2021
Copyright_xml – notice: The Author(s), under exclusive licence to Springer Nature Limited 2021. corrected publication 2021
– notice: 2021. The Author(s), under exclusive licence to Springer Nature Limited.
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These authors contributed equally: Qi Hu, Maria Victoria Botuyan, Debiao Zhao.
Author contributions G.M. conceived and supervised this work. G.M., Q.H., M.V.B. and D.Z. designed the experiments. Q.H. determined the cryo-EM structures. G.C. and Q.H. performed the NMR spectroscopy experiments. M.V.B. cLoned the different constructs. M.V.B., D.Z., Q.H. and E.M. produced and purified all samples. M.V.B., Q.H., D.Z. and E.M. performed the functional assays. G.M. wrote the manuscript with major contributions from M.V.B. and Q.H., and input from all authors.
ORCID 0000-0002-6466-7432
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References Stewart (CR30) 2009; 136
Moynahan, Chiu, Koller, Jasin (CR8) 1999; 4
Kalb, Mallery, Larkin, Huang, Hiom (CR13) 2014; 8
Hu (CR46) 2011; 25
Hall (CR1) 1990; 250
Benirschke (CR53) 2010; 18
Coleman, Greenberg (CR45) 2011; 286
Zivanov (CR63) 2018; 7
CR32
Hashizume (CR24) 2001; 276
Fradet-Turcotte (CR27) 2013; 499
Cui (CR50) 2010; 49
Chen (CR71) 2010; 66
Punjani, Fleet (CR35) 2021; 213
Lee, Tonelli, Markley (CR75) 2015; 31
Makde, England, Yennawar, Tan (CR57) 2010; 467
McGinty, Henrici, Tan (CR34) 2014; 514
Punjani, Rubinstein, Fleet, Brubaker (CR61) 2017; 14
Densham (CR14) 2016; 23
Su (CR54) 2011; 286
Matsumoto (CR58) 2019; 571
Luger, Rechsteiner, Richmond (CR56) 1999; 304
Futreal (CR3) 1994; 266
Scully (CR6) 1997; 88
Shukla (CR60) 2014; 512
Tan (CR65) 2017; 14
Brzovic, Rajagopal, Hoyt, King, Klevit (CR17) 2001; 8
Eddins, Carlile, Gomez, Pickart, Wolberger (CR41) 2006; 13
Sundd, Iverson, Ibarra-Molero, Sanchez-Ruiz, Robertson (CR49) 2002; 41
Zhao (CR7) 2017; 550
Billing (CR40) 2018; 72
Berndsen, Wolberger (CR51) 2011; 418
Doil (CR31) 2009; 136
Paull (CR37) 2000; 10
Mallery, Vandenberg, Hiom (CR25) 2002; 21
Liang (CR23) 2017; 3
Nakamura (CR11) 2019; 21
Mattiroli (CR15) 2012; 150
Berendsen, van der Spoel, van Drunen (CR77) 1995; 91
Fox (CR38) 2008; 283
Tarsounas, Sung (CR10) 2020; 21
Kim, Chen, Yu (CR44) 2007; 316
Witus (CR80) 2021; 28
Hu, Botuyan, Cui, Zhao, Mer (CR48) 2017; 66
Gatti (CR16) 2012; 11
Schanda, Kupce, Brutscher (CR76) 2005; 33
Stewart (CR26) 2018; 115
Delaglio (CR74) 1995; 6
Mukherjee (CR78) 2019; 33
Scheres (CR62) 2012; 180
Nakane, Kimanius, Lindahl, Scheres (CR36) 2018; 7
Sobhian (CR42) 2007; 316
Friedman (CR4) 1994; 8
Xu (CR47) 2010; 328
Chapman, Sossick, Boulton, Jackson (CR20) 2012; 125
Zheng (CR64) 2017; 14
Edwards (CR69) 2008; 47
Miki (CR2) 1994; 266
Li, Yu (CR39) 2013; 23
Greenberg (CR22) 2018; 20
Vijay-Kumar, Bugg, Cook (CR70) 1987; 194
Emsley, Cowtan (CR67) 2004; 60
Wilson (CR28) 2016; 536
Landrum (CR79) 2018; 46
Bouwman (CR19) 2010; 17
Botuyan (CR29) 2006; 127
Wu (CR5) 1996; 14
Birrane, Varma, Soni, Ladias (CR68) 2007; 46
Paull, Cortez, Bowers, Elledge, Gellert (CR9) 2001; 98
Pettersen (CR72) 2004; 25
Bentley (CR52) 2011; 30
Saredi (CR12) 2016; 534
Wang (CR43) 2007; 316
Bunting (CR18) 2010; 141
Liebschner (CR66) 2019; 75
Goddard (CR73) 2018; 27
Pellegrino, Michelena, Teloni, Imhof, Altmeyer (CR21) 2017; 19
Luger, Mäder, Richmond, Sargent, Richmond (CR33) 1997; 389
Su (CR55) 2012; 483
Marks (CR59) 2005; 3
CE Berndsen (3716_CR51) 2011; 418
D Fox III (3716_CR38) 2008; 283
TT Paull (3716_CR9) 2001; 98
A Fradet-Turcotte (3716_CR27) 2013; 499
LC Wu (3716_CR5) 1996; 14
A Punjani (3716_CR61) 2017; 14
VB Chen (3716_CR71) 2010; 66
SQ Zheng (3716_CR64) 2017; 14
Q Hu (3716_CR48) 2017; 66
RD Makde (3716_CR57) 2010; 467
DL Mallery (3716_CR25) 2002; 21
3716_CR32
JR Chapman (3716_CR20) 2012; 125
TT Paull (3716_CR37) 2000; 10
F Delaglio (3716_CR74) 1995; 6
GS Stewart (3716_CR30) 2009; 136
S Pellegrino (3716_CR21) 2017; 19
G Cui (3716_CR50) 2010; 49
W Zhao (3716_CR7) 2017; 550
KA Coleman (3716_CR45) 2011; 286
R Kalb (3716_CR13) 2014; 8
RM Densham (3716_CR14) 2016; 23
C Doil (3716_CR31) 2009; 136
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SH Scheres (3716_CR62) 2012; 180
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SF Bunting (3716_CR18) 2010; 141
W Lee (3716_CR75) 2015; 31
JM Hall (3716_CR1) 1990; 250
B Wang (3716_CR43) 2007; 316
Y Hu (3716_CR46) 2011; 25
S Vijay-Kumar (3716_CR70) 1987; 194
S Matsumoto (3716_CR58) 2019; 571
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SR Witus (3716_CR80) 2021; 28
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K Nakamura (3716_CR11) 2019; 21
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K Luger (3716_CR33) 1997; 389
R Scully (3716_CR6) 1997; 88
G Saredi (3716_CR12) 2016; 534
P Schanda (3716_CR76) 2005; 33
34404953 - Nature. 2021 Aug 17
References_xml – volume: 125
  start-page: 3529
  year: 2012
  end-page: 3534
  ident: CR20
  article-title: BRCA1-associated exclusion of 53BP1 from DNA damage sites underlies temporal control of DNA repair
  publication-title: J. Cell Sci.
– volume: 88
  start-page: 265
  year: 1997
  end-page: 275
  ident: CR6
  article-title: Association of BRCA1 with Rad51 in mitotic and meiotic cells
  publication-title: Cell
  doi: 10.1016/S0092-8674(00)81847-4
– volume: 23
  start-page: 693
  year: 2013
  end-page: 704
  ident: CR39
  article-title: Function of BRCA1 in the DNA damage response is mediated by ADP-ribosylation
  publication-title: Cancer Cell
  doi: 10.1016/j.ccr.2013.03.025
– volume: 28
  start-page: 268
  year: 2021
  end-page: 277
  ident: CR80
  article-title: BRCA1/BARD1 site-specific ubiquitylation of nucleosomal H2A is directed by BARD1
  publication-title: Nat. Struct. Mol. Biol.
  doi: 10.1038/s41594-020-00556-4
– volume: 7
  year: 2018
  ident: CR36
  article-title: Characterisation of molecular motions in cryo-EM single-particle data by multi-body refinement in RELION
  publication-title: eLife
  doi: 10.7554/eLife.36861
– volume: 389
  start-page: 251
  year: 1997
  end-page: 260
  ident: CR33
  article-title: Crystal structure of the nucleosome core particle at 2.8 A resolution
  publication-title: Nature
  doi: 10.1038/38444
– volume: 3
  year: 2017
  ident: CR23
  article-title: Structural analysis of BRCA1 reveals modification hotspot
  publication-title: Sci. Adv.
  doi: 10.1126/sciadv.1701386
– volume: 41
  start-page: 7586
  year: 2002
  end-page: 7596
  ident: CR49
  article-title: Electrostatic interactions in ubiquitin: stabilization of carboxylates by lysine amino groups
  publication-title: Biochemistry
  doi: 10.1021/bi025571d
– volume: 17
  start-page: 688
  year: 2010
  end-page: 695
  ident: CR19
  article-title: 53BP1 loss rescues BRCA1 deficiency and is associated with triple-negative and BRCA-mutated breast cancers
  publication-title: Nat. Struct. Mol. Biol.
  doi: 10.1038/nsmb.1831
– volume: 11
  start-page: 2538
  year: 2012
  end-page: 2544
  ident: CR16
  article-title: A novel ubiquitin mark at the N-terminal tail of histone H2As targeted by RNF168 ubiquitin ligase
  publication-title: Cell Cycle
  doi: 10.4161/cc.20919
– volume: 316
  start-page: 1198
  year: 2007
  end-page: 1202
  ident: CR42
  article-title: RAP80 targets BRCA1 to specific ubiquitin structures at DNA damage sites
  publication-title: Science
  doi: 10.1126/science.1139516
– volume: 571
  start-page: 79
  year: 2019
  end-page: 84
  ident: CR58
  article-title: DNA damage detection in nucleosomes involves DNA register shifting
  publication-title: Nature
  doi: 10.1038/s41586-019-1259-3
– volume: 33
  start-page: 199
  year: 2005
  end-page: 211
  ident: CR76
  article-title: SOFAST-HMQC experiments for recording two-dimensional heteronuclear correlation spectra of proteins within a few seconds
  publication-title: J. Biomol. NMR
  doi: 10.1007/s10858-005-4425-x
– volume: 25
  start-page: 1605
  year: 2004
  end-page: 1612
  ident: CR72
  article-title: UCSF Chimera—a visualization system for exploratory research and analysis
  publication-title: J. Comput. Chem.
  doi: 10.1002/jcc.20084
– volume: 276
  start-page: 14537
  year: 2001
  end-page: 14540
  ident: CR24
  article-title: The RING heterodimer BRCA1–BARD1 is a ubiquitin ligase inactivated by a breast cancer-derived mutation
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.C000881200
– volume: 20
  start-page: 862
  year: 2018
  end-page: 863
  ident: CR22
  article-title: Assembling a protective shield
  publication-title: Nat. Cell Biol.
  doi: 10.1038/s41556-018-0152-x
– volume: 98
  start-page: 6086
  year: 2001
  end-page: 6091
  ident: CR9
  article-title: Direct DNA binding by Brca1
  publication-title: Proc. Natl Acad. Sci. USA
  doi: 10.1073/pnas.111125998
– volume: 10
  start-page: 886
  year: 2000
  end-page: 895
  ident: CR37
  article-title: A critical role for histone H2AX in recruitment of repair factors to nuclear foci after DNA damage
  publication-title: Curr. Biol.
  doi: 10.1016/S0960-9822(00)00610-2
– volume: 8
  start-page: 999
  year: 2014
  end-page: 1005
  ident: CR13
  article-title: BRCA1 is a histone-H2A-specific ubiquitin ligase
  publication-title: Cell Rep.
  doi: 10.1016/j.celrep.2014.07.025
– volume: 66
  start-page: 12
  year: 2010
  end-page: 21
  ident: CR71
  article-title: MolProbity: all-atom structure validation for macromolecular crystallography
  publication-title: Acta Crystallogr. D
  doi: 10.1107/S0907444909042073
– volume: 75
  start-page: 861
  year: 2019
  end-page: 877
  ident: CR66
  article-title: Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix
  publication-title: Acta Crystallogr. D
  doi: 10.1107/S2059798319011471
– volume: 127
  start-page: 1361
  year: 2006
  end-page: 1373
  ident: CR29
  article-title: Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair
  publication-title: Cell
  doi: 10.1016/j.cell.2006.10.043
– volume: 136
  start-page: 420
  year: 2009
  end-page: 434
  ident: CR30
  article-title: The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling cascade at sites of DNA damage
  publication-title: Cell
  doi: 10.1016/j.cell.2008.12.042
– volume: 512
  start-page: 218
  year: 2014
  end-page: 222
  ident: CR60
  article-title: Visualization of arrestin recruitment by a G-protein-coupled receptor
  publication-title: Nature
  doi: 10.1038/nature13430
– volume: 283
  start-page: 21179
  year: 2008
  end-page: 21186
  ident: CR38
  article-title: Crystal structure of the BARD1 ankyrin repeat domain and its functional consequences
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M802333200
– volume: 30
  start-page: 3285
  year: 2011
  end-page: 3297
  ident: CR52
  article-title: Recognition of UbcH5c and the nucleosome by the Bmi1/Ring1b ubiquitin ligase complex
  publication-title: EMBO J.
  doi: 10.1038/emboj.2011.243
– volume: 266
  start-page: 120
  year: 1994
  end-page: 122
  ident: CR3
  article-title: BRCA1 mutations in primary breast and ovarian carcinomas
  publication-title: Science
  doi: 10.1126/science.7939630
– volume: 8
  start-page: 399
  year: 1994
  end-page: 404
  ident: CR4
  article-title: Confirmation of BRCA1 by analysis of germline mutations linked to breast and ovarian cancer in ten families
  publication-title: Nat. Genet.
  doi: 10.1038/ng1294-399
– volume: 21
  start-page: 284
  year: 2020
  end-page: 299
  ident: CR10
  article-title: The antitumorigenic roles of BRCA1–BARD1 in DNA repair and replication
  publication-title: Nat. Rev. Mol. Cell Biol.
  doi: 10.1038/s41580-020-0218-z
– volume: 4
  start-page: 511
  year: 1999
  end-page: 518
  ident: CR8
  article-title: Brca1 controls homology-directed DNA repair
  publication-title: Mol. Cell
  doi: 10.1016/S1097-2765(00)80202-6
– volume: 286
  start-page: 15625
  year: 2011
  end-page: 15629
  ident: CR54
  article-title: Structure and histone binding properties of the Vps75–Rtt109 chaperone–lysine acetyltransferase complex
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.C111.220715
– volume: 21
  start-page: 311
  year: 2019
  end-page: 318
  ident: CR11
  article-title: H4K20me0 recognition by BRCA1–BARD1 directs homologous recombination to sister chromatids
  publication-title: Nat. Cell Biol.
  doi: 10.1038/s41556-019-0282-9
– volume: 136
  start-page: 435
  year: 2009
  end-page: 446
  ident: CR31
  article-title: RNF168 binds and amplifies ubiquitin conjugates on damaged chromosomes to allow accumulation of repair proteins
  publication-title: Cell
  doi: 10.1016/j.cell.2008.12.041
– ident: CR32
– volume: 23
  start-page: 647
  year: 2016
  end-page: 655
  ident: CR14
  article-title: Human BRCA1–BARD1 ubiquitin ligase activity counteracts chromatin barriers to DNA resection
  publication-title: Nat. Struct. Mol. Biol.
  doi: 10.1038/nsmb.3236
– volume: 91
  start-page: 43
  year: 1995
  end-page: 56
  ident: CR77
  article-title: GROMACS: a message-passing parallel molecular dynamics implementation
  publication-title: Comput. Phys. Commun.
  doi: 10.1016/0010-4655(95)00042-E
– volume: 115
  start-page: 1316
  year: 2018
  end-page: 1321
  ident: CR26
  article-title: BARD1 is necessary for ubiquitylation of nucleosomal histone H2A and for transcriptional regulation of estrogen metabolism genes
  publication-title: Proc. Natl Acad. Sci. USA
  doi: 10.1073/pnas.1715467115
– volume: 180
  start-page: 519
  year: 2012
  end-page: 530
  ident: CR62
  article-title: RELION: implementation of a Bayesian approach to cryo-EM structure determination
  publication-title: J. Struct. Biol.
  doi: 10.1016/j.jsb.2012.09.006
– volume: 483
  start-page: 104
  year: 2012
  end-page: 107
  ident: CR55
  article-title: Structural basis for recognition of H3K56-acetylated histone H3–H4 by the chaperone Rtt106
  publication-title: Nature
  doi: 10.1038/nature10861
– volume: 33
  start-page: 1927
  year: 2019
  end-page: 1945
  ident: CR78
  article-title: Calmodulin regulates MGRN1–GP78 interaction mediated ubiquitin proteasomal degradation system
  publication-title: FASEB J.
  doi: 10.1096/fj.201701413RRR
– volume: 316
  start-page: 1202
  year: 2007
  end-page: 1205
  ident: CR44
  article-title: Ubiquitin-binding protein RAP80 mediates BRCA1-dependent DNA damage response
  publication-title: Science
  doi: 10.1126/science.1139621
– volume: 8
  start-page: 833
  year: 2001
  end-page: 837
  ident: CR17
  article-title: Structure of a BRCA1–BARD1 heterodimeric RING–RING complex
  publication-title: Nat. Struct. Biol.
  doi: 10.1038/nsb1001-833
– volume: 316
  start-page: 1194
  year: 2007
  end-page: 1198
  ident: CR43
  article-title: Abraxas and RAP80 form a BRCA1 protein complex required for the DNA damage response
  publication-title: Science
  doi: 10.1126/science.1139476
– volume: 27
  start-page: 14
  year: 2018
  end-page: 25
  ident: CR73
  article-title: UCSF ChimeraX: meeting modern challenges in visualization and analysis
  publication-title: Protein Sci.
  doi: 10.1002/pro.3235
– volume: 72
  start-page: 127
  year: 2018
  end-page: 139.e8
  ident: CR40
  article-title: The BRCT domains of the BRCA1 and BARD1 tumor suppressors differentially regulate homology-directed repair and stalled fork protection
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2018.08.016
– volume: 418
  start-page: 102
  year: 2011
  end-page: 110
  ident: CR51
  article-title: A spectrophotometric assay for conjugation of ubiquitin and ubiquitin-like proteins
  publication-title: Anal. Biochem.
  doi: 10.1016/j.ab.2011.06.034
– volume: 25
  start-page: 685
  year: 2011
  end-page: 700
  ident: CR46
  article-title: RAP80-directed tuning of BRCA1 homologous recombination function at ionizing radiation-induced nuclear foci
  publication-title: Genes Dev.
  doi: 10.1101/gad.2011011
– volume: 14
  start-page: 793
  year: 2017
  end-page: 796
  ident: CR65
  article-title: Addressing preferred specimen orientation in single-particle cryo-EM through tilting
  publication-title: Nat. Methods
  doi: 10.1038/nmeth.4347
– volume: 534
  start-page: 714
  year: 2016
  end-page: 718
  ident: CR12
  article-title: H4K20me0 marks post-replicative chromatin and recruits the TONSL–MMS22L DNA repair complex
  publication-title: Nature
  doi: 10.1038/nature18312
– volume: 3
  start-page: 613
  year: 2005
  end-page: 622
  ident: CR59
  article-title: Multiparameter analysis of a screen for progesterone receptor ligands: comparing fluorescence lifetime and fluorescence polarization measurements
  publication-title: Assay Drug Dev. Technol.
  doi: 10.1089/adt.2005.3.613
– volume: 18
  start-page: 955
  year: 2010
  end-page: 965
  ident: CR53
  article-title: Molecular basis for the association of human E4B U box ubiquitin ligase with E2-conjugating enzymes UbcH5c and Ubc4
  publication-title: Structure
  doi: 10.1016/j.str.2010.04.017
– volume: 6
  start-page: 277
  year: 1995
  end-page: 293
  ident: CR74
  article-title: NMRPipe: a multidimensional spectral processing system based on UNIX pipes
  publication-title: J. Biomol. NMR
  doi: 10.1007/BF00197809
– volume: 7
  year: 2018
  ident: CR63
  article-title: New tools for automated high-resolution cryo-EM structure determination in RELION-3
  publication-title: eLife
  doi: 10.7554/eLife.42166
– volume: 66
  start-page: 473
  year: 2017
  end-page: 487.e9
  ident: CR48
  article-title: Mechanisms of ubiquitin -nucleosome recognition and regulation of 53BP1 chromatin recruitment by RNF168/169 and RAD18
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2017.04.009
– volume: 304
  start-page: 3
  year: 1999
  end-page: 19
  ident: CR56
  article-title: Preparation of nucleosome core particle from recombinant histones
  publication-title: Methods Enzymol.
  doi: 10.1016/S0076-6879(99)04003-3
– volume: 19
  start-page: 1819
  year: 2017
  end-page: 1831
  ident: CR21
  article-title: Replication-coupled dilution of H4K20me2 guides 53BP1 to pre-replicative chromatin
  publication-title: Cell Rep.
  doi: 10.1016/j.celrep.2017.05.016
– volume: 550
  start-page: 360
  year: 2017
  end-page: 365
  ident: CR7
  article-title: BRCA1–BARD1 promotes RAD51-mediated homologous DNA pairing
  publication-title: Nature
  doi: 10.1038/nature24060
– volume: 60
  start-page: 2126
  year: 2004
  end-page: 2132
  ident: CR67
  article-title: Coot: model-building tools for molecular graphics
  publication-title: Acta Crystallogr. D
  doi: 10.1107/S0907444904019158
– volume: 21
  start-page: 6755
  year: 2002
  end-page: 6762
  ident: CR25
  article-title: Activation of the E3 ligase function of the BRCA1/BARD1 complex by polyubiquitin chains
  publication-title: EMBO J.
  doi: 10.1093/emboj/cdf691
– volume: 213
  start-page: 107702
  year: 2021
  ident: CR35
  article-title: 3D variability analysis: resolving continuous flexibility and discrete heterogeneity from single particle cryo-EM
  publication-title: J. Struct. Biol.
  doi: 10.1016/j.jsb.2021.107702
– volume: 46
  start-page: D1062
  year: 2018
  end-page: D1067
  ident: CR79
  article-title: ClinVar: improving access to variant interpretations and supporting evidence
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gkx1153
– volume: 47
  start-page: 11446
  year: 2008
  end-page: 11456
  ident: CR69
  article-title: The BARD1 C-terminal domain structure and interactions with polyadenylation factor CstF-50
  publication-title: Biochemistry
  doi: 10.1021/bi801115g
– volume: 31
  start-page: 1325
  year: 2015
  end-page: 1327
  ident: CR75
  article-title: NMRFAM-SPARKY: enhanced software for biomolecular NMR spectroscopy
  publication-title: Bioinformatics
  doi: 10.1093/bioinformatics/btu830
– volume: 141
  start-page: 243
  year: 2010
  end-page: 254
  ident: CR18
  article-title: 53BP1 inhibits homologous recombination in -deficient cells by blocking resection of DNA breaks
  publication-title: Cell
  doi: 10.1016/j.cell.2010.03.012
– volume: 14
  start-page: 290
  year: 2017
  end-page: 296
  ident: CR61
  article-title: cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination
  publication-title: Nat. Methods
  doi: 10.1038/nmeth.4169
– volume: 150
  start-page: 1182
  year: 2012
  end-page: 1195
  ident: CR15
  article-title: RNF168 ubiquitinates K13-15 on H2A/H2AX to drive DNA damage signaling
  publication-title: Cell
  doi: 10.1016/j.cell.2012.08.005
– volume: 13
  start-page: 915
  year: 2006
  end-page: 920
  ident: CR41
  article-title: Mms2–Ubc13 covalently bound to ubiquitin reveals the structural basis of linkage-specific polyubiquitin chain formation
  publication-title: Nat. Struct. Mol. Biol.
  doi: 10.1038/nsmb1148
– volume: 49
  start-page: 10198
  year: 2010
  end-page: 10207
  ident: CR50
  article-title: Structural basis of ubiquitin recognition by translesion synthesis DNA polymerase ι
  publication-title: Biochemistry
  doi: 10.1021/bi101303t
– volume: 286
  start-page: 13669
  year: 2011
  end-page: 13680
  ident: CR45
  article-title: The BRCA1–RAP80 complex regulates DNA repair mechanism utilization by restricting end resection
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M110.213728
– volume: 14
  start-page: 331
  year: 2017
  end-page: 332
  ident: CR64
  article-title: MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy
  publication-title: Nat. Methods
  doi: 10.1038/nmeth.4193
– volume: 536
  start-page: 100
  year: 2016
  end-page: 103
  ident: CR28
  article-title: The structural basis of modified nucleosome recognition by 53BP1
  publication-title: Nature
  doi: 10.1038/nature18951
– volume: 467
  start-page: 562
  year: 2010
  end-page: 566
  ident: CR57
  article-title: Structure of RCC1 chromatin factor bound to the nucleosome core particle
  publication-title: Nature
  doi: 10.1038/nature09321
– volume: 499
  start-page: 50
  year: 2013
  end-page: 54
  ident: CR27
  article-title: 53BP1 is a reader of the DNA-damage-induced H2A Lys 15 ubiquitin mark
  publication-title: Nature
  doi: 10.1038/nature12318
– volume: 328
  start-page: 94
  year: 2010
  end-page: 98
  ident: CR47
  article-title: Partitioning of histone H3–H4 tetramers during DNA replication-dependent chromatin assembly
  publication-title: Science
  doi: 10.1126/science.1178994
– volume: 266
  start-page: 66
  year: 1994
  end-page: 71
  ident: CR2
  article-title: A strong candidate for the breast and ovarian cancer susceptibility gene BRCA1
  publication-title: Science
  doi: 10.1126/science.7545954
– volume: 14
  start-page: 430
  year: 1996
  end-page: 440
  ident: CR5
  article-title: Identification of a RING protein that can interact in vivo with the BRCA1 gene product
  publication-title: Nat. Genet.
  doi: 10.1038/ng1296-430
– volume: 250
  start-page: 1684
  year: 1990
  end-page: 1689
  ident: CR1
  article-title: Linkage of early-onset familial breast cancer to chromosome 17q21
  publication-title: Science
  doi: 10.1126/science.2270482
– volume: 514
  start-page: 591
  year: 2014
  end-page: 596
  ident: CR34
  article-title: Crystal structure of the PRC1 ubiquitylation module bound to the nucleosome
  publication-title: Nature
  doi: 10.1038/nature13890
– volume: 194
  start-page: 531
  year: 1987
  end-page: 544
  ident: CR70
  article-title: Structure of ubiquitin refined at 1.8 A resolution
  publication-title: J. Mol. Biol.
  doi: 10.1016/0022-2836(87)90679-6
– volume: 46
  start-page: 7706
  year: 2007
  end-page: 7712
  ident: CR68
  article-title: Crystal structure of the BARD1 BRCT domains
  publication-title: Biochemistry
  doi: 10.1021/bi700323t
– volume: 550
  start-page: 360
  year: 2017
  ident: 3716_CR7
  publication-title: Nature
  doi: 10.1038/nature24060
– volume: 31
  start-page: 1325
  year: 2015
  ident: 3716_CR75
  publication-title: Bioinformatics
  doi: 10.1093/bioinformatics/btu830
– volume: 512
  start-page: 218
  year: 2014
  ident: 3716_CR60
  publication-title: Nature
  doi: 10.1038/nature13430
– volume: 11
  start-page: 2538
  year: 2012
  ident: 3716_CR16
  publication-title: Cell Cycle
  doi: 10.4161/cc.20919
– volume: 8
  start-page: 833
  year: 2001
  ident: 3716_CR17
  publication-title: Nat. Struct. Biol.
  doi: 10.1038/nsb1001-833
– volume: 3
  year: 2017
  ident: 3716_CR23
  publication-title: Sci. Adv.
  doi: 10.1126/sciadv.1701386
– volume: 23
  start-page: 693
  year: 2013
  ident: 3716_CR39
  publication-title: Cancer Cell
  doi: 10.1016/j.ccr.2013.03.025
– volume: 571
  start-page: 79
  year: 2019
  ident: 3716_CR58
  publication-title: Nature
  doi: 10.1038/s41586-019-1259-3
– volume: 136
  start-page: 420
  year: 2009
  ident: 3716_CR30
  publication-title: Cell
  doi: 10.1016/j.cell.2008.12.042
– volume: 41
  start-page: 7586
  year: 2002
  ident: 3716_CR49
  publication-title: Biochemistry
  doi: 10.1021/bi025571d
– volume: 23
  start-page: 647
  year: 2016
  ident: 3716_CR14
  publication-title: Nat. Struct. Mol. Biol.
  doi: 10.1038/nsmb.3236
– volume: 467
  start-page: 562
  year: 2010
  ident: 3716_CR57
  publication-title: Nature
  doi: 10.1038/nature09321
– volume: 17
  start-page: 688
  year: 2010
  ident: 3716_CR19
  publication-title: Nat. Struct. Mol. Biol.
  doi: 10.1038/nsmb.1831
– volume: 316
  start-page: 1202
  year: 2007
  ident: 3716_CR44
  publication-title: Science
  doi: 10.1126/science.1139621
– volume: 3
  start-page: 613
  year: 2005
  ident: 3716_CR59
  publication-title: Assay Drug Dev. Technol.
  doi: 10.1089/adt.2005.3.613
– volume: 14
  start-page: 793
  year: 2017
  ident: 3716_CR65
  publication-title: Nat. Methods
  doi: 10.1038/nmeth.4347
– volume: 14
  start-page: 331
  year: 2017
  ident: 3716_CR64
  publication-title: Nat. Methods
  doi: 10.1038/nmeth.4193
– volume: 21
  start-page: 284
  year: 2020
  ident: 3716_CR10
  publication-title: Nat. Rev. Mol. Cell Biol.
  doi: 10.1038/s41580-020-0218-z
– volume: 21
  start-page: 311
  year: 2019
  ident: 3716_CR11
  publication-title: Nat. Cell Biol.
  doi: 10.1038/s41556-019-0282-9
– volume: 30
  start-page: 3285
  year: 2011
  ident: 3716_CR52
  publication-title: EMBO J.
  doi: 10.1038/emboj.2011.243
– volume: 14
  start-page: 290
  year: 2017
  ident: 3716_CR61
  publication-title: Nat. Methods
  doi: 10.1038/nmeth.4169
– volume: 33
  start-page: 199
  year: 2005
  ident: 3716_CR76
  publication-title: J. Biomol. NMR
  doi: 10.1007/s10858-005-4425-x
– volume: 33
  start-page: 1927
  year: 2019
  ident: 3716_CR78
  publication-title: FASEB J.
  doi: 10.1096/fj.201701413RRR
– volume: 46
  start-page: D1062
  year: 2018
  ident: 3716_CR79
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gkx1153
– volume: 276
  start-page: 14537
  year: 2001
  ident: 3716_CR24
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.C000881200
– volume: 127
  start-page: 1361
  year: 2006
  ident: 3716_CR29
  publication-title: Cell
  doi: 10.1016/j.cell.2006.10.043
– volume: 8
  start-page: 399
  year: 1994
  ident: 3716_CR4
  publication-title: Nat. Genet.
  doi: 10.1038/ng1294-399
– volume: 20
  start-page: 862
  year: 2018
  ident: 3716_CR22
  publication-title: Nat. Cell Biol.
  doi: 10.1038/s41556-018-0152-x
– volume: 75
  start-page: 861
  year: 2019
  ident: 3716_CR66
  publication-title: Acta Crystallogr. D
  doi: 10.1107/S2059798319011471
– volume: 304
  start-page: 3
  year: 1999
  ident: 3716_CR56
  publication-title: Methods Enzymol.
  doi: 10.1016/S0076-6879(99)04003-3
– volume: 125
  start-page: 3529
  year: 2012
  ident: 3716_CR20
  publication-title: J. Cell Sci.
  doi: 10.1242/jcs.105353
– volume: 21
  start-page: 6755
  year: 2002
  ident: 3716_CR25
  publication-title: EMBO J.
  doi: 10.1093/emboj/cdf691
– volume: 4
  start-page: 511
  year: 1999
  ident: 3716_CR8
  publication-title: Mol. Cell
  doi: 10.1016/S1097-2765(00)80202-6
– volume: 88
  start-page: 265
  year: 1997
  ident: 3716_CR6
  publication-title: Cell
  doi: 10.1016/S0092-8674(00)81847-4
– volume: 72
  start-page: 127
  year: 2018
  ident: 3716_CR40
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2018.08.016
– volume: 316
  start-page: 1194
  year: 2007
  ident: 3716_CR43
  publication-title: Science
  doi: 10.1126/science.1139476
– volume: 499
  start-page: 50
  year: 2013
  ident: 3716_CR27
  publication-title: Nature
  doi: 10.1038/nature12318
– volume: 250
  start-page: 1684
  year: 1990
  ident: 3716_CR1
  publication-title: Science
  doi: 10.1126/science.2270482
– volume: 27
  start-page: 14
  year: 2018
  ident: 3716_CR73
  publication-title: Protein Sci.
  doi: 10.1002/pro.3235
– ident: 3716_CR32
  doi: 10.1101/2020.06.01.127951
– volume: 14
  start-page: 430
  year: 1996
  ident: 3716_CR5
  publication-title: Nat. Genet.
  doi: 10.1038/ng1296-430
– volume: 141
  start-page: 243
  year: 2010
  ident: 3716_CR18
  publication-title: Cell
  doi: 10.1016/j.cell.2010.03.012
– volume: 66
  start-page: 12
  year: 2010
  ident: 3716_CR71
  publication-title: Acta Crystallogr. D
  doi: 10.1107/S0907444909042073
– volume: 13
  start-page: 915
  year: 2006
  ident: 3716_CR41
  publication-title: Nat. Struct. Mol. Biol.
  doi: 10.1038/nsmb1148
– volume: 286
  start-page: 15625
  year: 2011
  ident: 3716_CR54
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.C111.220715
– volume: 10
  start-page: 886
  year: 2000
  ident: 3716_CR37
  publication-title: Curr. Biol.
  doi: 10.1016/S0960-9822(00)00610-2
– volume: 286
  start-page: 13669
  year: 2011
  ident: 3716_CR45
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M110.213728
– volume: 47
  start-page: 11446
  year: 2008
  ident: 3716_CR69
  publication-title: Biochemistry
  doi: 10.1021/bi801115g
– volume: 7
  year: 2018
  ident: 3716_CR36
  publication-title: eLife
  doi: 10.7554/eLife.36861
– volume: 213
  start-page: 107702
  year: 2021
  ident: 3716_CR35
  publication-title: J. Struct. Biol.
  doi: 10.1016/j.jsb.2021.107702
– volume: 6
  start-page: 277
  year: 1995
  ident: 3716_CR74
  publication-title: J. Biomol. NMR
  doi: 10.1007/BF00197809
– volume: 266
  start-page: 120
  year: 1994
  ident: 3716_CR3
  publication-title: Science
  doi: 10.1126/science.7939630
– volume: 28
  start-page: 268
  year: 2021
  ident: 3716_CR80
  publication-title: Nat. Struct. Mol. Biol.
  doi: 10.1038/s41594-020-00556-4
– volume: 180
  start-page: 519
  year: 2012
  ident: 3716_CR62
  publication-title: J. Struct. Biol.
  doi: 10.1016/j.jsb.2012.09.006
– volume: 115
  start-page: 1316
  year: 2018
  ident: 3716_CR26
  publication-title: Proc. Natl Acad. Sci. USA
  doi: 10.1073/pnas.1715467115
– volume: 8
  start-page: 999
  year: 2014
  ident: 3716_CR13
  publication-title: Cell Rep.
  doi: 10.1016/j.celrep.2014.07.025
– volume: 328
  start-page: 94
  year: 2010
  ident: 3716_CR47
  publication-title: Science
  doi: 10.1126/science.1178994
– volume: 418
  start-page: 102
  year: 2011
  ident: 3716_CR51
  publication-title: Anal. Biochem.
  doi: 10.1016/j.ab.2011.06.034
– volume: 7
  year: 2018
  ident: 3716_CR63
  publication-title: eLife
  doi: 10.7554/eLife.42166
– volume: 91
  start-page: 43
  year: 1995
  ident: 3716_CR77
  publication-title: Comput. Phys. Commun.
  doi: 10.1016/0010-4655(95)00042-E
– volume: 60
  start-page: 2126
  year: 2004
  ident: 3716_CR67
  publication-title: Acta Crystallogr. D
  doi: 10.1107/S0907444904019158
– volume: 316
  start-page: 1198
  year: 2007
  ident: 3716_CR42
  publication-title: Science
  doi: 10.1126/science.1139516
– volume: 49
  start-page: 10198
  year: 2010
  ident: 3716_CR50
  publication-title: Biochemistry
  doi: 10.1021/bi101303t
– volume: 25
  start-page: 1605
  year: 2004
  ident: 3716_CR72
  publication-title: J. Comput. Chem.
  doi: 10.1002/jcc.20084
– volume: 534
  start-page: 714
  year: 2016
  ident: 3716_CR12
  publication-title: Nature
  doi: 10.1038/nature18312
– volume: 98
  start-page: 6086
  year: 2001
  ident: 3716_CR9
  publication-title: Proc. Natl Acad. Sci. USA
  doi: 10.1073/pnas.111125998
– volume: 46
  start-page: 7706
  year: 2007
  ident: 3716_CR68
  publication-title: Biochemistry
  doi: 10.1021/bi700323t
– volume: 483
  start-page: 104
  year: 2012
  ident: 3716_CR55
  publication-title: Nature
  doi: 10.1038/nature10861
– volume: 19
  start-page: 1819
  year: 2017
  ident: 3716_CR21
  publication-title: Cell Rep.
  doi: 10.1016/j.celrep.2017.05.016
– volume: 25
  start-page: 685
  year: 2011
  ident: 3716_CR46
  publication-title: Genes Dev.
  doi: 10.1101/gad.2011011
– volume: 18
  start-page: 955
  year: 2010
  ident: 3716_CR53
  publication-title: Structure
  doi: 10.1016/j.str.2010.04.017
– volume: 150
  start-page: 1182
  year: 2012
  ident: 3716_CR15
  publication-title: Cell
  doi: 10.1016/j.cell.2012.08.005
– volume: 66
  start-page: 473
  year: 2017
  ident: 3716_CR48
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2017.04.009
– volume: 266
  start-page: 66
  year: 1994
  ident: 3716_CR2
  publication-title: Science
  doi: 10.1126/science.7545954
– volume: 283
  start-page: 21179
  year: 2008
  ident: 3716_CR38
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M802333200
– volume: 389
  start-page: 251
  year: 1997
  ident: 3716_CR33
  publication-title: Nature
  doi: 10.1038/38444
– volume: 136
  start-page: 435
  year: 2009
  ident: 3716_CR31
  publication-title: Cell
  doi: 10.1016/j.cell.2008.12.041
– volume: 536
  start-page: 100
  year: 2016
  ident: 3716_CR28
  publication-title: Nature
  doi: 10.1038/nature18951
– volume: 194
  start-page: 531
  year: 1987
  ident: 3716_CR70
  publication-title: J. Mol. Biol.
  doi: 10.1016/0022-2836(87)90679-6
– volume: 514
  start-page: 591
  year: 2014
  ident: 3716_CR34
  publication-title: Nature
  doi: 10.1038/nature13890
– reference: 34404953 - Nature. 2021 Aug 17;:
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Snippet The BRCA1–BARD1 tumour suppressor is an E3 ubiquitin ligase necessary for the repair of DNA double-strand breaks by homologous recombination 1 – 10 . The...
The BRCA1-BARD1 tumour suppressor is an E3 ubiquitin ligase necessary for the repair of DNA double-strand breaks by homologous recombination . The BRCA1-BARD1...
The BRCA1-BARD1 tumour suppressor is an E3 ubiquitin ligase necessary for the repair of DNA double-strand breaks by homologous recombination.sup.1-10. The...
The BRCA1-BARD1 tumour suppressor is an E3 ubiquitin ligase necessary for the repair ofDNA double-strand breaks by homologous recombination. The BRCA1-BARD1...
The BRCA1-BARD1 tumour suppressor is an E3 ubiquitin ligase necessary for the repair of DNA double-strand breaks by homologous recombination1-10. The...
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Publisher
StartPage 438
SubjectTerms 101/28
101/6
631/337/100/1701
631/337/1427/2122
631/337/458/582
631/535/1258/1259
631/535/878/1263
82
82/16
82/6
82/80
82/83
Amino acids
Ankyrins
BRCA1 protein
BRCA1 Protein - metabolism
Breast cancer
C-Terminus
Cancer
Chromatin
Crosstalk
Cryoelectron Microscopy
Damage localization
Deoxyribonucleic acid
DNA
DNA biosynthesis
DNA Repair
Domains
Electron microscopy
Enzymes
Flexibility
Genetic aspects
Histone H2A
Histones
Histones - chemistry
Histones - metabolism
Homologous Recombination
Homology
Humanities and Social Sciences
Humans
Microscopy
Models, Molecular
multidisciplinary
Mutation
Neoplasms - genetics
NMR
Nuclear magnetic resonance
Nucleosomes
Nucleosomes - chemistry
Nucleosomes - genetics
Nucleosomes - metabolism
Nucleosomes - ultrastructure
Physiological aspects
Protein Domains
Proteins
Recruitment
Repair
Science
Science (multidisciplinary)
Spectrum analysis
Target recognition
Tumor suppressor genes
Tumor Suppressor p53-Binding Protein 1 - antagonists & inhibitors
Tumor Suppressor p53-Binding Protein 1 - metabolism
Tumor Suppressor Proteins - chemistry
Tumor Suppressor Proteins - genetics
Tumor Suppressor Proteins - metabolism
Tumor Suppressor Proteins - ultrastructure
Tumors
Ubiquitin
Ubiquitin - metabolism
Ubiquitin-conjugating enzyme
Ubiquitin-Conjugating Enzymes - chemistry
Ubiquitin-Conjugating Enzymes - metabolism
Ubiquitin-Conjugating Enzymes - ultrastructure
Ubiquitin-protein ligase
Ubiquitin-Protein Ligases - chemistry
Ubiquitin-Protein Ligases - genetics
Ubiquitin-Protein Ligases - metabolism
Ubiquitin-Protein Ligases - ultrastructure
Ubiquitination
Title Mechanisms of BRCA1–BARD1 nucleosome recognition and ubiquitylation
URI https://link.springer.com/article/10.1038/s41586-021-03716-8
https://www.ncbi.nlm.nih.gov/pubmed/34321665
https://www.proquest.com/docview/2563499899
https://www.proquest.com/docview/2556383327
https://pubmed.ncbi.nlm.nih.gov/PMC8680157
Volume 596
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