The human checkpoint sensor and alternative DNA clamp Rad9–Rad1–Hus1 modulates the activity of DNA ligase I, a component of the long-patch base excision repair machinery
Copyright policy )The human checkpoint sensor and alternative DNA clamp Rad9–Rad1–Hus1 modulates the activity of DNA ligase I, a component of the long-patch base excision repair machinery
The human checkpoint sensor and alternative clamp Rad9–Rad1–Hus1 can interact with and specifically stimulate DNA ligase I. The very recently described interactions of Rad9–Rad1–Hus1 with MutY DNA glycosylase, DNA polymerase β and Flap endonuclease 1 now complete our view that the long-patch base excision machinery is an important target of the Rad9–Rad1–Hus1 complex, thus enhancing the quality control of DNA.
- University of Zurich Switzerland
Exonucleases, 1303 Biochemistry, DNA Ligases, DNA Repair, Cell Cycle Proteins, 10226 Department of Molecular Mechanisms of Disease, 1307 Cell Biology, Enzyme Activation, DNA Ligase ATP, Multiprotein Complexes, Proliferating Cell Nuclear Antigen, 1312 Molecular Biology, 570 Life sciences; biology, Humans, Schizosaccharomyces pombe Proteins, DNA Damage, Protein Binding
Exonucleases, 1303 Biochemistry, DNA Ligases, DNA Repair, Cell Cycle Proteins, 10226 Department of Molecular Mechanisms of Disease, 1307 Cell Biology, Enzyme Activation, DNA Ligase ATP, Multiprotein Complexes, Proliferating Cell Nuclear Antigen, 1312 Molecular Biology, 570 Life sciences; biology, Humans, Schizosaccharomyces pombe Proteins, DNA Damage, Protein Binding
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