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PMID:15871698

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Citation

Smirnova, E, Toueille, M, Markkanen, E and Hübscher, U (2005) 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. Biochem. J. 389:13-7

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.

Links

PubMed PMC1184534 Online version:10.1042/BJ20050211

Keywords

Cell Cycle Proteins/metabolism; DNA Damage; 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

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

HUMAN:DNLI1

GO:0003909: DNA ligase activity

ECO:0000315:

F

Data for DNA ligase activity in homo sapiens is shown in Figure 3.

complete
CACAO 5277

HUMAN:DNLI1

enables

GO:0003909: DNA ligase activity

ECO:0000315: mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete


See also

References

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