Unraveling the Base Excision Repair Mechanism of Human DNA Glycosylase

2015 ◽  
Vol 137 (31) ◽  
pp. 9824-9831 ◽  
Author(s):  
Keyarash Sadeghian ◽  
Christian Ochsenfeld
Keyword(s):  
Base Excision Repair ◽  
Excision Repair ◽  
Dna Glycosylase ◽  
Repair Mechanism ◽  
Human Dna ◽  
Base Excision

scholarly journals Base excision repair and design of small molecule inhibitors of human DNA polymerase β

2010 ◽  
Vol 67 (21) ◽  
pp. 3633-3647 ◽  
Author(s):  
Samuel H. Wilson ◽  
William A. Beard ◽  
David D. Shock ◽  
Vinod K. Batra ◽  
Nisha A. Cavanaugh ◽  
...  
Keyword(s):  
Dna Polymerase ◽  
Small Molecule ◽  
Base Excision Repair ◽  
Small Molecule Inhibitors ◽  
Excision Repair ◽  
Dna Polymerase Β ◽  
Human Dna ◽  
Base Excision

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.

Human DNA polymerase λ catalyzes lesion bypass across benzo[a]pyrene-derived DNA adduct during base excision repair

DNA Repair ◽  
2012 ◽  
Vol 11 (4) ◽  
pp. 367-373 ◽  
Author(s):  
Lidia V. Skosareva ◽  
Natalia A. Lebedeva ◽  
Nadejda I. Rechkunova ◽  
Alexander Kolbanovskiy ◽  
Nicholas E. Geacintov ◽  
...  
Keyword(s):  
Dna Polymerase ◽  
Base Excision Repair ◽  
Excision Repair ◽  
Dna Adduct ◽  
Lesion Bypass ◽  
Human Dna ◽  
Dna Polymerase Λ ◽  
Base Excision

scholarly journals The Domains of Mammalian Base Excision Repair EnzymeN-Methylpurine-DNA Glycosylase

1996 ◽  
Vol 271 (39) ◽  
pp. 23690-23697 ◽  
Author(s):  
Rabindra Roy ◽  
Amalendra Kumar ◽  
J. Ching Lee ◽  
Sankar Mitra
Keyword(s):  
Base Excision Repair ◽  
Excision Repair ◽  
Dna Glycosylase ◽  
Methylpurine Dna Glycosylase ◽  
Base Excision
Sign in / Sign up

Export Citation Format

Share Document