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The cruciform DNA‐binding protein Crp1 stimulates the endonuclease activity of Mus81–Mms4 inSaccharomyces cerevisiae
- Source :
- FEBS Letters. 594:4320-4337
- Publication Year :
- 2020
- Publisher :
- Wiley, 2020.
-
Abstract
- 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.
- Subjects :
- Saccharomyces cerevisiae Proteins
Flap Endonucleases
DNA repair
Saccharomyces cerevisiae
Mutant
Biophysics
Biochemistry
DNA-binding protein
03 medical and health sciences
Endonuclease
chemistry.chemical_compound
Protein Domains
Structural Biology
Gene Expression Regulation, Fungal
Genetics
Molecular Biology
030304 developmental biology
DNA, Cruciform
0303 health sciences
RecQ Helicases
biology
030302 biochemistry & molecular biology
Cell Biology
Endonucleases
biology.organism_classification
MUS81
Cell biology
DNA-Binding Proteins
Enzyme Activation
Kinetics
chemistry
Cruciform
Mutation
biology.protein
Nucleic Acid Conformation
DNA
Protein Binding
Subjects
Details
- ISSN :
- 18733468 and 00145793
- Volume :
- 594
- Database :
- OpenAIRE
- Journal :
- FEBS Letters
- Accession number :
- edsair.doi.dedup.....3928dc9ef819333023d8bc26f1f8ddfc