Repair of O6-Methylguanine by ABC Excinuclease of Escherichia coli in vitro

Voigt, Jeffrey M.; Houten, Ben Van; Sancar, Aziz; Topal, Michael D.

doi:10.1016/s0021-9258(18)83715-2

Cited by 91 publications

(32 citation statements)

References 18 publications

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“…This is likely to be the case with mammalian excision nuclease(s) as well, because rats excrete thymidine glycol and thymine glycol in their urine (Catchart et al, 1984), which are presumably released from DNA by an excision nuclease and a DNA glycosylase, respectively. Finally, the observations reported in this paper bring into focus once more the substrate specificity of (A)BC excinuclease [see Voigt et al (1989)]. Two of the well-investigated substrates, the thymine dimer and the dr-Pt-GG diadduct, induce a 30-40°bend into the major groove (Pearlman et al, 1985;Husain et al, 1988;Rice et al, 1988) while a psoralen cross-link appears to bend DNA by some assays (Tomic et al, 1987;Shi et al, 1988) but not by others (Haran & Crothers, 1988).…”

Section: Discussionmentioning

confidence: 88%

“…E. coli mutants defective in C^-mGua DNA methyltransferase have increased sensitivity to MNNG when they are also defective in (A)BC excinuclease (Van Houten & Sancar, 1987;Samson et al, 1988;Rossi et al, 1989). Furthermore, it has been shown that the purified enzyme excises (T'-mGuA from DNA (Voigt et al, 1989). Similarly, Saporito et al (1989) were able to construct xth nfo, xth uvrA, nfo uvrA double mutants but not the xth nfo uvrA triple mutant, suggesting a functional redundancy of the three proteins which is probably the removal of AP sites, although alternative explanations are also possible.…”

Section: Discussionmentioning

confidence: 99%

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A new mechanism for repairing oxidative damage to DNA: (A)BC excinuclease removes AP sites and thymine glycols from DNA

Lin¹,

Sancar²

1989

Biochemistry

183

100

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Escherichia coli (A)BC excinuclease is the major enzyme responsible for removing bulky adducts, such as pyrimidine dimers and 6-4 photoproducts, from DNA. Mutants deficient in this enzyme are extremely sensitive to UV and UV-mimetic agents, but not to oxidizing agents, or ionizing radiation which damages DNA in part by generating active oxygen species. DNA glycosylases and AP1 endonucleases play major roles in repairing oxidative DNA damage, and thus it has been assumed that nucleotide excision repair has no role in cellular defense against damage by ionizing radiation and oxidative damage. In this study we show that the E. coli nucleotide excision repair enzyme (A)BC excinuclease removes from DNA the two major products of oxidative damage, thymine glycol and the baseless sugar (AP site). We conclude that nucleotide excision repair is an important cellular defense mechanism against oxidizing agents.

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Section: Discussionmentioning

confidence: 88%

Section: Discussionmentioning

confidence: 99%

A new mechanism for repairing oxidative damage to DNA: (A)BC excinuclease removes AP sites and thymine glycols from DNA

Lin¹,

Sancar²

1989

Biochemistry

183

100

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“…Similar 5Ј-hypersensitive sites in the damtunity to verify that the lesion is really a substrate for aged strand were observed upon complex formation of NER. In addition, the XPA protein may help to organize the E. coli UvrAB repair proteins with various lesions and correctly orient the NER machinery around the DNA (Van Houten et al, 1987;Voigt et al, 1989;Visse et al, injury. Further research using a purified set of NER pro-1991).…”

Section: Xpc-hr23b Was Stably Sequestered By Preincubation a Two-stage Damage Recognitionmentioning

confidence: 99%

Xeroderma Pigmentosum Group C Protein Complex Is the Initiator of Global Genome Nucleotide Excision Repair

et al. 1998

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The XPC-HR23B complex is specifically involved in global genome but not transcription-coupled nucleotide excision repair (NER). Its function is unknown. Using a novel DNA damage recognition-competition assay, we identified XPC-HR23B as the earliest damage detector to initiate NER: it acts before the known damage-binding protein XPA. Coimmunoprecipitation and DNase I footprinting show that XPC-HR23B binds to a variety of NER lesions. These results resolve the function of XPC-HR23B, define the first NER stages, and suggest a two-step mechanism of damage recognition involving damage detection by XPC-HR23B followed by damage verification by XPA. This provides a plausible explanation for the extreme damage specificity exhibited by global genome repair. In analogy, in the transcription-coupled NER subpathway, RNA polymerase II may take the role of XPC. After this subpathway-specific initial lesion detection, XPA may function as a common damage verifier and adaptor to the core of the NER apparatus.

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“…In addition to the methyltransferases, the UvrABC nucleotide excision repair (NER) pathway can also repair O 6 MeG. Excision of O 6 MeG on duplex substrates has been shown to occur in vitro (28) and in vivo (29). When O 6 MeG is present in a single-stranded context in vivo, NER does not affect mutation frequency of the lesion; the mutation frequencies in E.coli uvrB þ ada À ogt À cells are very similar to those found in uvrB À ada À ogt À cells (30).…”

Section: Introductionmentioning

confidence: 99%

Chemical biology of mutagenesis and DNA repair: cellular responses to DNA alkylation

2009

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The reaction of DNA-damaging agents with the genome results in a plethora of lesions, commonly referred to as adducts. Adducts may cause DNA to mutate, they may represent the chemical precursors of lethal events and they can disrupt expression of genes. Determination of which adduct is responsible for each of these biological endpoints is difficult, but this task has been accomplished for some carcinogenic DNA-damaging agents. Here, we describe the respective contributions of specific DNA lesions to the biological effects of low molecular weight alkylating agents.

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Repair of O6-Methylguanine by ABC Excinuclease of Escherichia coli in vitro

Cited by 91 publications

References 18 publications

A new mechanism for repairing oxidative damage to DNA: (A)BC excinuclease removes AP sites and thymine glycols from DNA

A new mechanism for repairing oxidative damage to DNA: (A)BC excinuclease removes AP sites and thymine glycols from DNA

Xeroderma Pigmentosum Group C Protein Complex Is the Initiator of Global Genome Nucleotide Excision Repair

Chemical biology of mutagenesis and DNA repair: cellular responses to DNA alkylation

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