Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair.

By M. Botuyan, Joseph Lee, Irene M. Ward, Ja-Eun Kim, J. Thompson, Junjie Chen, G. Mer. Cell, 2006

1,027 citations recorded by the source corpus.

Subfields: Analytical Chemistry, Biophysics, Ecology

View Paper: https://www.semanticscholar.org/paper/a211fd9613a861d432ca6b609d9843c40abe51df

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Citations in the corpus

RIF1 Is Essential for 53BP1-Dependent Nonhomologous End Joining and Suppression of DNA Double-Strand Break Resection (2013, background): “53BP1 contains closely opposed homo-oligomerization and tandem Tudor domains that are both required for its interaction Molecular Cell 49, 858–871, March 7, 2013 ª2013 Elsevier Inc. 863 with nucleosomes at DSB sites (Botuyan et al., 2006; Huyen et al., 2004; Zgheib et al., 2009).”
How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickers (2007, background): “; for recognition of lower methylation states (me2 and me1), hydrogen-bonding and steric exclusion are increasingly importan”
More than just a focus: The chromatin response to DNA damage and its role in genome integrity maintenance (2011, background): “However, both histone methylations associated with 53BP1 chromatin retention (H3K79me and H4K20me) have been considered as constitutive, which suggests that repositioning of nucleosomes after DNA damage exposes these otherwise hidden methylation mark”
53BP1 is a reader of the DNA damage-induced H2A Lys15 ubiquitin mark (2013, methodology): “The retroviral vector pMX-53BP1 (1-1711) and its D1521R derivative were gifts of André Nussenzweig9.”
Mechanism and regulation of class switch recombination. (2008, background): “Mammalian 53BP1 binds dimethyl-lysine 20 of histone H4 (H4-K20-me2), but not mono- or trimethyl K20, via its Tudor domains (164).”
Playing the end game: DNA double-strand break repair pathway choice. (2012, background): “Indeed, 53BP1 binds dimethyl-histone H4 Lys20 (H4K20me2) (Botuyan et al., 2006), and this is crucial for limiting the resection of the DSB intermediates of CSR and V(D)J recombination (Bothmer et al., 2010; Difilippantonio et al., 2008).”
DNA damage-induced alterations in chromatin contribute to genomic integrity and age-related changes in gene expression (2008, positive): “SIRT1 Is Recruited to DSBs and Is Required for Efficient DNA Repair A role for chromatin modifiers in DNA repair has been convincingly shown in yeast and mammals (Tamburini and Tyler, 2005; Bassing et al., 2002; Bhaskara et al., 2008; Botuyan et al., 2006; Celeste et al., 2002; Xie et al., 2004).”
The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling cascade at sites of DNA damage. (2009, positive): “By contrast, 53BP1 does not possess ubiquitin-binding domains, and its localization to DNA damage sites, rather, depends on its Tudor domain, a methyl-lysine residuebinding module (Botuyan et al., 2006; Huyen et al., 2004).”
Dynamics of DNA damage response proteins at DNA breaks: a focus on protein modifications. (2011, background): “2007), while human 53BP1 was initially reported to bind H3K79me3 and subsequently H4K20me1/2 (mono or dimethylated), which might be more physiologically relevant (Huyen et al. 2004; Botuyan et al. 2006; Oda et al. 2010).”
RNF168 binds and amplifies ubiquitin conjugates on damaged chromosomes to allow accumulation of repair proteins. (2009, positive): “Furthermore, accumulation of 53BP1 at DSBs requires also constitutive epigenetic marks (such as dimethylatedK79ofhistoneH3and/ordimethylatedK20ofhistone H4), which are recognized by the Tudor domain of 53BP1 ( Botuyan et al., 2006; Huyen et al., 2004).”