Rtt107 BRCT domains act as a targeting module in the DNA damage response

摘要: Cells are constantly exposed to assaults that cause DNA damage, which must be detected and repaired prevent genome instability. The damage response is mediated by key kinases activate various signaling pathways. In Saccharomyces cerevisiae, one of these Mec1, phosphorylates numerous targets, including H2A the protein Rtt107. addition being phosphorylated, Rtt107 contains six BRCA1 C-terminal (BRCT) domains, typically recognize phospho-peptides. Thus represented an opportunity study complementary aspects phosphorylation cascades within protein. Here we sought describe functional roles multiple BRCT domains in BRCT5/6 facilitated recruitment sites lesions via its interaction with phosphorylated H2A. BRCT3/4 also contributed recruitment, but was not sufficient for when absent. Intriguingly, both mutations affected abrogated phosphorylation. Pointing modular nature, replacing from checkpoint Rad9 able sustain function. Although physically interacts endonuclease Slx4 replication repair Dpb11, only dependent on lesions. Fusing Slx4, presumably allows artificial lesions, alleviated some phenotypes rtt107Δ mutants, indicating importance recruitment. Together this data revealed a function targeting itself partners