Fpg protein of Escherichia coli is a zinc finger protein whose cysteine residues have a structural and/or functional role.

O’Connor, Tim; Graves, Robert J.; Murcia, Gilbert de; Castaing, B.; Laval, Jacques

doi:10.1016/s0021-9258(18)52978-1

Cited by 139 publications

(16 citation statements)

References 32 publications

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“…Rats placed on a zinc-deficient diet and the offspring of zinc-deficient rhesus monkeys both have a higher incidence of chromosome breaks 111,112 . These chromosome breaks seem to be caused by oxidative damage 111,113 , which could result from a loss of activity of copper-zinc superoxide dismutase or formamidopyrimidine glycosylase -a zinc-containing DNA-repair enzyme that repairs oxidized guanine 114 .…”

Section: Discussionmentioning

confidence: 99%

Are vitamin and mineral deficiencies a major cancer risk?

Ames¹,

Wakimoto²

2002

Nat Rev Cancer

250

214

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Diet is estimated to contribute to about one-third of preventable cancers -- about the same amount as smoking. Inadequate intake of essential vitamins and minerals might explain the epidemiological findings that people who eat only small amounts of fruits and vegetables have an increased risk of developing cancer. Recent experimental evidence indicates that vitamin and mineral deficiencies can lead to DNA damage. Optimizing vitamin and mineral intake by encouraging dietary change, multivitamin and mineral supplements, and fortifying foods might therefore prevent cancer and other chronic diseases.

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Section: Discussionmentioning

confidence: 99%

Are vitamin and mineral deficiencies a major cancer risk?

Ames¹,

Wakimoto²

2002

Nat Rev Cancer

250

214

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“…identified a putative Cys 2 His 2 -type zinc finger motif adjacent to the HhH and they suggest that this potential DNA binding motif may function in concert with the HhH in a manner analogous to the FCL motif in endo III and MutY. Notably, the FPG protein which is more distantly related to the BER superfamily 14 has a Cys 4 zinc finger motif at its C-terminus. , The presence of the zinc finger motif in the FPG protein is critical for DNA binding and the glycosylase/lyase activity. This again suggests that different DNA binding motifs may coordinate to effect DNA recognition.…”

Section: Fe−s Cluster Loop Domain Of Endo III and Mutymentioning

confidence: 98%

“…Notably, the FPG protein which is more distantly related to the BER superfamily 14 has a Cys 4 zinc finger motif at its C-terminus. 214,215 The presence of the zinc finger motif in the FPG protein is critical for DNA binding and the glycosylase/lyase activity. This again suggests that different DNA binding motifs may coordinate to effect DNA recognition.…”

Section: Fe−s Cluster Loop Domain Of Endo III and Mutymentioning

confidence: 99%

Chemistry of Glycosylases and Endonucleases Involved in Base-Excision Repair

1998

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ContentsI. Introduction 1221 II. Types of Base-Excision Repair Glycosylases 1223 A. Uracil-DNA Glycosylase (UDG) 1223 B. Mismatch-Specific Thymine-DNA Glycosylase (TDG) and Related Double-Strand Specific Uracil DNA Glycosylase (dsUDG) 1226 C. Alkylated Base Removal 1227 D. Endonuclease III and Related Enzymes 1229 E. Pyrimidine Dimer Glycosylases 1230 F. The FPG Protein (Fapy Glycosylase or MutM) 1231

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“…H2TH superfamily DNA glycosylases comprise two domains connected by a flexible linker; the active site is formed by residues from both domains [9]. The C-terminal half of the catalytic domain of many H2TH glycosylases (E. coli Fpg and Nei, human NEIL2 and NEIL3) is equipped with a prominent structural feature identified as a Cys 4 -type zinc finger in earlier works [70,71]. The X-ray structures [72,73] show that this part belongs to the β ribbon class of zinc fingers [74] (Figure 3A).…”

Section: Zinc-binding Structural Motifsmentioning

confidence: 99%

Noncatalytic Domains in DNA Glycosylases

Torgasheva

Diatlova

Grin

et al. 2022

IJMS

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Many proteins consist of two or more structural domains: separate parts that have a defined structure and function. For example, in enzymes, the catalytic activity is often localized in a core fragment, while other domains or disordered parts of the same protein participate in a number of regulatory processes. This situation is often observed in many DNA glycosylases, the proteins that remove damaged nucleobases thus initiating base excision DNA repair. This review covers the present knowledge about the functions and evolution of such noncatalytic parts in DNA glycosylases, mostly concerned with the human enzymes but also considering some unique members of this group coming from plants and prokaryotes.

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Fpg protein of Escherichia coli is a zinc finger protein whose cysteine residues have a structural and/or functional role.

Cited by 139 publications

References 32 publications

Are vitamin and mineral deficiencies a major cancer risk?

Are vitamin and mineral deficiencies a major cancer risk?

Chemistry of Glycosylases and Endonucleases Involved in Base-Excision Repair

Noncatalytic Domains in DNA Glycosylases

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