Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand breaks (Q28291639)

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Omar Zgheib

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Richard A Ditullio

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Vassilis G Gorgoulis

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Panayotis Zacharatos

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Tom J Petty

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Emily A Sheston

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Hestia S Mellert

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Elena S Stavridi

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Thanos D Halazonetis

Role for the silencing protein Dot1 in meiotic checkpoint control

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language of work or name

English

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publication date

18 November 2004

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published in

Nature

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volume

432

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issue

7015

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page(s)

406-11

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cites work

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p53 binding protein 1 (53BP1) is an early participant in the cellular response to DNA double-strand breaks

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Negative cell cycle regulation and DNA damage-inducible phosphorylation of the BRCT protein 53BP1.

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Phosphorylation and rapid relocalization of 53BP1 to nuclear foci upon DNA damage

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Tumor suppressor p53 binding protein 1 (53BP1) is involved in DNA damage-signaling pathways

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Accumulation of Checkpoint Protein 53BP1 at DNA Breaks Involves Its Binding to Phosphorylated Histone H2AX

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Potential role for 53BP1 in DNA end-joining repair through direct interaction with DNA.

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The RAD9 gene controls the cell cycle response to DNA damage in Saccharomyces cerevisiae

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Isolation and characterization of the Schizosaccharomyces pombe rhp9 gene: a gene required for the DNA damage checkpoint but not the replication checkpoint

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Damage and replication checkpoint control in fission yeast is ensured by interactions of Crb2, a protein with BRCT motif, with Cut5 and Chk1.

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Combined functional genomic maps of the C. elegans DNA damage response

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The Tudor tandem of 53BP1: a new structural motif involved in DNA and RG-rich peptide binding

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SMN tudor domain structure and its interaction with the Sm proteins

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High-resolution X-ray and NMR structures of the SMN Tudor domain: conformational variation in the binding site for symmetrically dimethylated arginine residues

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Nucleic acid recognition by OB-fold proteins

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SMN, the product of the spinal muscular atrophy gene, binds preferentially to dimethylarginine-containing protein targets

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Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B' and the Sm-like protein LSm4, and their interaction with the SMN protein.

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Histone methylation in transcriptional control

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Methylation of H3-lysine 79 is mediated by a new family of HMTases without a SET domain

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Dot1p modulates silencing in yeast by methylation of the nucleosome core

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Disruptor of telomeric silencing-1 is a chromatin-specific histone H3 methyltransferase.

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Megabase chromatin domains involved in DNA double-strand breaks in vivo

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DNA damage activates ATM through intermolecular autophosphorylation and dimer dissociation

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Histone H2AX phosphorylation is dispensable for the initial recognition of DNA breaks

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Crystal structure of the nucleosome core particle at 2.8 A resolution

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Nucleosome gaping supports a functional structure for the 30nm chromatin fiber.

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Structural differences in the DNA binding domains of human p53 and its C. elegans ortholog Cep-1.

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Interaction of human DNA polymerase eta with monoubiquitinated PCNA: a possible mechanism for the polymerase switch in response to DNA damage

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