Cleavage of Insertion/Deletion Mismatches, Flap and Pseudo-Y DNA Structures by Deoxyinosine 3′-Endonuclease from Escherichia coli*

@article{Yao1996CleavageOI,
  title={Cleavage of Insertion/Deletion Mismatches, Flap and Pseudo-Y DNA Structures by Deoxyinosine 3′-Endonuclease from Escherichia coli*},
  author={Ming Dong Yao and Yoke Wah Kow},
  journal={The Journal of Biological Chemistry},
  year={1996},
  volume={271},
  pages={30672 - 30676}
}
  • M. Yao, Y. Kow
  • Published 29 November 1996
  • Biology, Chemistry
  • The Journal of Biological Chemistry
Deoxyinosine 3′-endonuclease, an Escherichia coli repair enzyme that recognizes and cleaves DNA containing deoxyinosine and base mismatches, can cleave heteroduplexes containing a hairpin or unpaired loop. These DNA structures, referred to as insertion/deletion mismatches (IDM), are abnormal intermediate structures generated during replication of repetitive DNA sequences. In addition, the enzyme also cleaved the 5′-single-stranded tails of flap and pseudo-Y DNA structures, suggesting that… 

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References

SHOWING 1-10 OF 32 REFERENCES
Strand-specific cleavage of mismatch-containing DNA by deoxyinosine 3'-endonuclease from Escherichia coli.
  • M. Yao, Y. Kow
  • Biology, Chemistry
    The Journal of biological chemistry
  • 1994
TLDR
Interestingly, deoxyinosine 3'endonuclease showed strong strand specificity on DNA containing mismatches, and only one strand of the mismatch-containing DNA was nicked by the enzyme, and this strand specificity of mismatch cleavage was not affected by the nature of the mismatches.
Functional domains within FEN-1 and RAD2 define a family of structure-specific endonucleases: implications for nucleotide excision repair.
TLDR
The cloning of the murine FEN-1 gene is described and it is shown that YKL510 and a truncated RAD2 protein are also structure-specific endonucleases and implicates branched DNA structures as important intermediates in nucleotide excision repair.
Interaction of Deoxyinosine 3′-Endonuclease from Escherichia coli with DNA Containing Deoxyinosine (*)
  • M. Yao, Y. Kow
  • Biology, Chemistry
    The Journal of Biological Chemistry
  • 1995
TLDR
Deoxyinosine 3′-endonuclease exhibited similar affinities for both the substrate and the nicked duplex product and thus remained bound to the DNA after the cleavage reaction, and a model is proposed for the interaction of deoxyinosinesine 3″-endonUClease with DNA containing de Oxyinosine.
Lagging Strand DNA Synthesis at the Eukaryotic Replication Fork Involves Binding and Stimulation of FEN-1 by Proliferating Cell Nuclear Antigen (*)
TLDR
It is reported that FEN-1 physically interacts with proliferating cell nuclear antigen (PCNA), the processivity factor for DNA polymerases and .
Gene conversion in Escherichia coli: the recF pathway for resolution of heteroduplex DNA
TLDR
Heteroduplex plasmid DNAs are constructed and purified that contain heteroallelic 10-base-pair insertion-deletion mismatches that are similar in structure to the heterod uplex DNA intermediates that have been proposed to be produced during the genetic recombination of plasmids.
Structure-specific endonucleolytic cleavage of nucleic acids by eubacterial DNA polymerases.
TLDR
Any linear single-stranded nucleic acid can be targeted for specific cleavage by the 5' nuclease of DNA polymerase through hybridization with an oligonucleotide that converts the desired cleavage site into a substrate.
The characterization of a mammalian DNA structure‐specific endonuclease.
TLDR
This assay has allowed the first purification of a mammalian DNA structure‐specific nuclease in mammalian nuclear extracts and described here, flap endonuclease‐1 (FEN‐1), cleaves DNA flap strands that terminate with a 5′ single‐stranded end.
A 5' to 3' exonuclease functionally interacts with calf DNA polymerase epsilon.
Analysis of fractions containing purified DNA polymerase epsilon from calf thymus has revealed the presence of a 5' to 3' exonuclease activity that is specific for a single strand of duplex DNA. This
...
1
2
3
4
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