A role for Saccharomyces cerevisiae histone H2A in DNA repair

By J. Downs, N. Lowndes, Stephen P. Jackson. Nature, 2000

717 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/1604750f4624e815b3b51e684361f8c0983e891e

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In Molecular Biology

Citations in the corpus

Phosphorylation-dependent assembly of DNA damage response systems and the central roles of TOPBP1 (2021, background): “Comparable phosphorylations of closely related C-terminal motifs are also observed in both of the yeast species commonly used in genome stability studies, Saccharomyces cerevisiae [4] and Schizosaccharomyces pombe [5] but here the phosphorylation occurs on the normal histone H2A isoform rather than ”
γ-H2AX in recognition and signaling of DNA double-strand breaks in the context of chromatin (2008, background): “The first report that suggested a role for H2AX in DNA repair was a genetic study in yeast (53).”
Recruitment of the INO80 complex by H2A phosphorylation links ATP-dependent chromatin remodeling with DNA double-strand break repair. (2004, neutral): “Phosphorylated H2AX, re- (Downs et al., 2000) and the INO80 complex (Figure 2) ferred to as -H2AX, forms foci that appear to be a both impair NHEJ efficiency.”
Surviving the breakup: the DNA damage checkpoint. (2006, background): “both fungal and animal cells and is required for full viability of yeast and animal cells in the presence of DNA damaging agents (17, 18, 36, 102, 116).”
Acetylation of histone H4 by Esa1 is required for DNA double-strand break repair (2002, background): “The code may be complex because H2A phosphorylation also seems to be involved in NHE”
Dynamics of DNA damage response proteins at DNA breaks: a focus on protein modifications. (2011, background): “More generally, it appears that there is a conserved mechanism for apical DDR kinase recruitment to DNA damage sites that involves similar interaction motifs in the C termini of human Ku80-, NBS1-, and ATRIP-mediating interactions with DNA-PKcs, ATM, and ATR, respectively (Falck et al. 2005).”
Histone H2AX phosphorylation is dispensable for the initial recognition of DNA breaks (2003, background): “Both Ser residues were simultaneously mutated to Ala (S136A/S139A) to eliminate phosphorylation, or to Glu (S136E/S139E) to mimic constitutive phosphorylatio”