scholarly journals Association of Dnmt3a and thymine DNA glycosylase links DNA methylation with base-excision repair

2006 ◽  
Vol 35 (2) ◽  
pp. 390-400 ◽  
Author(s):  
Ya-Qiang Li ◽  
Ping-Zhu Zhou ◽  
Xiu-Dan Zheng ◽  
Colum P. Walsh ◽  
Guo-Liang Xu
Keyword(s):  
Dna Methylation ◽  
Base Excision Repair ◽  
Excision Repair ◽  
Dna Glycosylase ◽  
Thymine Dna Glycosylase ◽  
Base Excision

scholarly journals The Hepatitis B Virus X Protein Inhibits Thymine DNA Glycosylase Initiated Base Excision Repair

PLoS ONE ◽  
2012 ◽  
Vol 7 (11) ◽  
pp. e48940 ◽  
Author(s):  
Maarten A. A. van de Klundert ◽  
Formijn J. van Hemert ◽  
Hans L. Zaaijer ◽  
Neeltje A. Kootstra
Keyword(s):  
Hepatitis B Virus ◽  
Hepatitis B ◽  
Base Excision Repair ◽  
Excision Repair ◽  
Dna Glycosylase ◽  
X Protein ◽  
Thymine Dna Glycosylase ◽  
B Virus ◽  
Base Excision

scholarly journals Thymine DNA glycosylase modulates DNA damage response and gene expression by base excision repair-dependent and independent mechanisms

2017 ◽  
Vol 22 (4) ◽  
pp. 392-405 ◽  
Author(s):  
Tomohumi Nakamura ◽  
Kouichi Murakami ◽  
Haruto Tada ◽  
Yoshihiko Uehara ◽  
Jumpei Nogami ◽  
...  
Keyword(s):  
Gene Expression ◽  
Dna Damage ◽  
Dna Damage Response ◽  
Base Excision Repair ◽  
Excision Repair ◽  
Dna Glycosylase ◽  
Thymine Dna Glycosylase ◽  
Damage Response ◽  
Base Excision

scholarly journals Thymine DNA Glycosylase Is Essential for Active DNA Demethylation by Linked Deamination-Base Excision Repair

Cell ◽  
2011 ◽  
Vol 146 (1) ◽  
pp. 67-79 ◽  
Author(s):  
Salvatore Cortellino ◽  
Jinfei Xu ◽  
Mara Sannai ◽  
Robert Moore ◽  
Elena Caretti ◽  
...  
Keyword(s):  
Base Excision Repair ◽  
Excision Repair ◽  
Dna Demethylation ◽  
Dna Glycosylase ◽  
Thymine Dna Glycosylase ◽  
Active Dna Demethylation ◽  
Base Excision

scholarly journals Thymine DNA Glycosylase Can Rapidly Excise 5-Formylcytosine and 5-Carboxylcytosine

2011 ◽  
Vol 286 (41) ◽  
pp. 35334-35338 ◽  
Author(s):  
Atanu Maiti ◽  
Alexander C. Drohat
Keyword(s):  
Embryonic Development ◽  
Catalytic Mechanism ◽  
Excision Repair ◽  
Dna Demethylation ◽  
Oxidation Products ◽  
Dna Glycosylase ◽  
Thymine Dna Glycosylase ◽  
Active Demethylation ◽  
Active Dna Demethylation ◽  
Base Excision

Thymine DNA glycosylase (TDG) excises T from G·T mispairs and is thought to initiate base excision repair (BER) of deaminated 5-methylcytosine (mC). Recent studies show that TDG, including its glycosylase activity, is essential for active DNA demethylation and embryonic development. These and other findings suggest that active demethylation could involve mC deamination by a deaminase, giving a G·T mispair followed by TDG-initiated BER. An alternative proposal is that demethylation could involve iterative oxidation of mC to 5-hydroxymethylcytosine (hmC) and then to 5-formylcytosine (fC) and 5-carboxylcytosine (caC), mediated by a Tet (ten eleven translocation) enzyme, with conversion of caC to C by a putative decarboxylase. Our previous studies suggest that TDG could excise fC and caC from DNA, which could provide another potential demethylation mechanism. We show here that TDG rapidly removes fC, with higher activity than for G·T mispairs, and has substantial caC excision activity, yet it cannot remove hmC. TDG excision of fC and caC, oxidation products of mC, is consistent with its strong specificity for excising bases from a CpG context. Our findings reveal a remarkable new aspect of specificity for TDG, inform its catalytic mechanism, and suggest that TDG could protect against fC-induced mutagenesis. The results also suggest a new potential mechanism for active DNA demethylation, involving TDG excision of Tet-produced fC (or caC) and subsequent BER. Such a mechanism obviates the need for a decarboxylase and is consistent with findings that TDG glycosylase activity is essential for active demethylation and embryonic development, as are mechanisms involving TDG excision of deaminated mC or hmC.

scholarly journals Multiprobe RNase Protection Assay Analysis of mRNA Levels for the Escherichia coli Oxidative DNA Glycosylase Genes under Conditions of Oxidative Stress

2000 ◽  
Vol 182 (19) ◽  
pp. 5416-5424 ◽  
Author(s):  
Christine M. Gifford ◽  
Jeffrey O. Blaisdell ◽  
Susan S. Wallace
Keyword(s):  
Escherichia Coli ◽  
Base Excision Repair ◽  
Excision Repair ◽  
Dna Glycosylase ◽  
Mrna Levels ◽  
Aerobic Growth ◽  
Rnase Protection ◽  
Transcript Levels ◽  
Endonuclease Iii ◽  
Base Excision

ABSTRACT Escherichia coli formamidopyrimidine DNA glycosylase (Fpg), MutY DNA glycosylase, endonuclease VIII, and endonuclease III are oxidative base excision repair DNA glycosylases that remove oxidized bases from DNA, or an incorrect base paired with an oxidized base in the case of MutY. Since genes encoding other base excision repair proteins have been shown to be part of adaptive responses inE. coli, we wanted to determine whether the oxidative DNA glycosylase genes are induced in response to conditions that cause the type of damage their encoded proteins remove. The genesfpg, mutY, nei, and nthencode Fpg, MutY, endonuclease VIII, and endonuclease III, respectively. Multiprobe RNase protection assays were used to examine the transcript levels of these genes under conditions that induce the SoxRS, OxyR, and SOS regulons after a shift from anaerobic to aerobic growth and at different stages along the growth curve. Transcript levels for all four genes decreased as cells progressed from log-phase growth to stationary phase and increased after cells were shifted from anaerobic to aerobic growth. None of the genes were induced by hydrogen peroxide, paraquat, X rays, or conditions that induce the SOS response.

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