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Mechanism of 5′-Directed Excision in Human Mismatch Repair
- Source :
- Molecular Cell. 12(5):1077-1086
- Publication Year :
- 2003
- Publisher :
- Elsevier BV, 2003.
-
Abstract
- We have developed a purified system that supports mismatch-dependent 5'--3' excision. In the presence of RPA, ATP, and a mismatch, MutSalpha activates 5'--3' excision by EXOI, and excision terminates after removal of the mispair. MutSalpha confers high processivity on EXOI, and termination is due to RPA-dependent displacement of this processive complex from the helix and a weak ability of EXOI to reload at the RPA-bound gap in the product, as well as MutSalpha- and MutLalpha-dependent suppression of EXOI activity in the absence of a mismatch cofactor. As observed in the purified system, excision directed by a 5' strand break in HeLa nuclear extract can proceed in the absence of MutLalpha or PCNA, although 3' excision in the extract system requires both proteins.
- Subjects :
- DNA Repair
Base Pair Mismatch
Exonuclease 1
Adenosine Triphosphate
Bacterial Proteins
Replication Protein A
Humans
Molecular Biology
Genetics
Adenosine Triphosphatases
Cell Nucleus
biology
Escherichia coli Proteins
Processivity
DNA
Cell Biology
MutS DNA Mismatch-Binding Protein
Proliferating cell nuclear antigen
Cell biology
DNA-Binding Proteins
Enzyme Activation
DNA Repair Enzymes
Exodeoxyribonucleases
MutL Proteins
biology.protein
DNA mismatch repair
HeLa Cells
Subjects
Details
- ISSN :
- 10972765
- Volume :
- 12
- Issue :
- 5
- Database :
- OpenAIRE
- Journal :
- Molecular Cell
- Accession number :
- edsair.doi.dedup.....000e8a1f1761fae35d7253e91a67f3ea
- Full Text :
- https://doi.org/10.1016/s1097-2765(03)00428-3