Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Cell Cycle Proteins / metabolism*
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DNA Damage
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DNA Ligase ATP
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DNA Ligases / metabolism*
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DNA Repair / physiology*
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Enzyme Activation
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Exonucleases / metabolism*
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Humans
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Multiprotein Complexes / metabolism
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Proliferating Cell Nuclear Antigen / metabolism
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Protein Binding
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Schizosaccharomyces pombe Proteins / metabolism*
Substances
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Cell Cycle Proteins
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LIG1 protein, human
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Multiprotein Complexes
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Proliferating Cell Nuclear Antigen
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Schizosaccharomyces pombe Proteins
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hus1 protein, S pombe
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rad9 protein
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Exonucleases
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Rad1 protein, human
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DNA Ligases
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DNA Ligase ATP