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 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 beta and Flap endonuclease 1 now complete our view that the long-patch base...

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Bibliographic Details
Published in:Biochemical journal Vol. 389; no. Pt 1; pp. 13 - 17
Main Authors: Smirnova, Ekaterina, Toueille, Magali, Markkanen, Enni, Hübscher, Ulrich
Format: Journal Article
Language:English
Published: England Portland Press Ltd 01-07-2005
Subjects:
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Cell Cycle Proteins - metabolism
DNA Damage
DNA Ligase ATP
DNA Ligases - metabolism
DNA Repair - physiology
Enzyme Activation
Exonucleases - metabolism
Humans
Multiprotein Complexes - metabolism
Proliferating Cell Nuclear Antigen - metabolism
Protein Binding
Schizosaccharomyces pombe Proteins - metabolism
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Summary: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 beta 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.
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ISSN:0264-6021
1470-8728
DOI:10.1042/bj20050211