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The cruciform DNA‐binding protein Crp1 stimulates the endonuclease activity of Mus81–Mms4 in Saccharomyces cerevisiae
Author(s) -
Phung Huong Thi Thu,
Tran Diem Hong,
Nguyen Ta Xuan
Publication year - 2020
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13931
Subject(s) - cruciform , saccharomyces cerevisiae , endonuclease , biology , microbiology and biotechnology , dna , dna repair , homologous recombination , gene , genetics , history , archaeology
The Saccharomyces cerevisiae Mus81–Mms4 complex is a highly conserved DNA structure‐specific endonuclease that plays essential roles in the processing of recombination intermediates that arise during the repair of stalled replication forks and double‐stranded breaks. To identify novel factors functioning conjointly with Mus81–Mms4, we performed a biochemical screen and found that Crp1, a cruciform DNA‐recognizing protein that specifically binds to DNA four‐way junction structures, could stimulate the Mus81–Mms4 endonuclease. The specific protein interaction between Mus81–Mms4 and Crp1 was responsible for the stimulation observed. Multicopy expression of Crp1 could partially rescue the sensitivity to DNA‐damaging agents of the sgs1∆mus81∆21‐24N mutant. Our results provide insight into the functional role and interaction of Crp1 with other proteins involved in DNA repair.