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Literature DB >> 1445834

A repair system for 8-oxo-7,8-dihydrodeoxyguanine.

M L Michaels¹, J Tchou, A P Grollman, J H Miller.

Abstract

Active oxygen species can damage DNA and may play a role in aging and carcinogenesis. We have tested MutY glycosylase for activity on undamaged mispairs as well as mispairs formed with the oxidatively damaged substrates, 8-oxo-7,8-dihydrodeoxyguanine (GO) or 8-oxo-7,8-dihydrodeoxyadenine (AO). MutY acts as a glycosylase on four of the heteroduplexes tested, A/G, A/GO, A/C, and A/AO, removing the undamaged adenine from each substrate. Genetic data suggest that the primary substrate for MutY glycosylase in vivo is the A/GO mispair. We present biochemical evidence demonstrating that MutY glycosylase is an important part of a repair system that includes the MutM and MutT proteins. The GO repair system is dedicated to the repair of the oxidatively damaged guanine and the mutations it can induce.

Entities: Chemical Disease Gene

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Year: 1992 PMID： 1445834 DOI： 10.1021/bi00160a004

Source DB: PubMed Journal: Biochemistry ISSN： 0006-2960 Impact factor: 3.162

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Cited

111 in total

1. A novel role for Escherichia coli endonuclease VIII in prevention of spontaneous G-->T transversions.

Authors: J O Blaisdell; Z Hatahet; S S Wallace
Journal: J Bacteriol Date: 1999-10 Impact factor: 3.490

2. Functional expression of hMYH, a human homolog of the Escherichia coli MutY protein.

Authors: M M Slupska; W M Luther; J H Chiang; H Yang; J H Miller
Journal: J Bacteriol Date: 1999-10 Impact factor: 3.490

3. Efficient recognition of substrates and substrate analogs by the adenine glycosylase MutY requires the C-terminal domain.

Authors: N H Chmiel; M P Golinelli; A W Francis; S S David
Journal: Nucleic Acids Res Date: 2001-01-15 Impact factor: 16.971

4. The genes encoding formamidopyrimidine and MutY DNA glycosylases in Escherichia coli are transcribed as part of complex operons.

Authors: C M Gifford; S S Wallace
Journal: J Bacteriol Date: 1999-07 Impact factor: 3.490

5. Intact MutY and its catalytic domain differentially contact with A/8-oxoG-containing DNA.

Authors: X Li; A L Lu
Journal: Nucleic Acids Res Date: 2000-12-01 Impact factor: 16.971

6. Crystal structure of a repair enzyme of oxidatively damaged DNA, MutM (Fpg), from an extreme thermophile, Thermus thermophilus HB8.

Authors: M Sugahara; T Mikawa; T Kumasaka; M Yamamoto; R Kato; K Fukuyama; Y Inoue; S Kuramitsu
Journal: EMBO J Date: 2000-08-01 Impact factor: 11.598

A repair system for 8-oxo-7,8-dihydrodeoxyguanine.

1. A novel role for Escherichia coli endonuclease VIII in prevention of spontaneous G-->T transversions.

2. Functional expression of hMYH, a human homolog of the Escherichia coli MutY protein.

3. Efficient recognition of substrates and substrate analogs by the adenine glycosylase MutY requires the C-terminal domain.

4. The genes encoding formamidopyrimidine and MutY DNA glycosylases in Escherichia coli are transcribed as part of complex operons.

5. Intact MutY and its catalytic domain differentially contact with A/8-oxoG-containing DNA.

6. Crystal structure of a repair enzyme of oxidatively damaged DNA, MutM (Fpg), from an extreme thermophile, Thermus thermophilus HB8.

7. Protection from superoxide damage associated with an increased level of the YggX protein in Salmonella enterica.

8. The Escherichia coli methyl-directed mismatch repair system repairs base pairs containing oxidative lesions.

Review 9. DNA glycosylases in the base excision repair of DNA.

10. Cloning and characterization of hOGG1, a human homolog of the OGG1 gene of Saccharomyces cerevisiae.