IndraLab

Statements


| 4

sparser
"By contrast, Rap1 binding to DNA through a single Myb-like domain results in formation of high stoichiometry complexes that act at DNA ends mostly in a Rif2-independent manner."

sparser
"Based on the available crystal structures, with such a short DNA duplex it is difficult to rationalize how Rap1 DBD would be able to bind with both Myb-like domains interacting with the DNA."

sparser
"In fact, a characterization of Rap1 mutant variants shows that Rap1 binding to DNA through both Myb-like domains results in formation of Rap1-DNA complexes that control MRX functions at both DSBs and telomeres primarily through Rif2."

sparser
"MRX association at DSBs is counteracted by Rif2, which is known to interact with Rap1 that binds telomeric DNA through two tandem Myb-like domains."