Sequence Context- and Temperature-Dependent Nucleotide Excision Repair of a Benzo[a]pyrene Diol Epoxide-Guanine DNA Adduct Catalyzed by Thermophilic UvrABC Proteins†

Biochemistry ◽  
2007 ◽  
Vol 46 (23) ◽  
pp. 7006-7015 ◽  
Author(s):  
Qian Ruan ◽  
Tongming Liu ◽  
Alexander Kolbanovskiy ◽  
Yang Liu ◽  
Jian Ren ◽  
...  
Keyword(s):  
Nucleotide Excision Repair ◽  
Excision Repair ◽  
Dna Adduct ◽  
Temperature Dependent ◽  
Sequence Context ◽  
Diol Epoxide ◽  
Nucleotide Excision

Role of Base Sequence Context in Conformational Equilibria and Nucleotide Excision Repair of Benzo[a]pyrene Diol Epoxide−Adenine Adducts†

Biochemistry ◽  
2003 ◽  
Vol 42 (8) ◽  
pp. 2339-2354 ◽  
Author(s):  
Shixiang Yan ◽  
Min Wu ◽  
Tonko Buterin ◽  
Hanspeter Naegeli ◽  
Nicholas E. Geacintov ◽  
...  
Keyword(s):  
Nucleotide Excision Repair ◽  
Excision Repair ◽  
Base Sequence ◽  
Sequence Context ◽  
Diol Epoxide ◽  
Nucleotide Excision ◽  
Conformational Equilibria ◽  
Adenine Adducts

scholarly journals Variation in PAH-related DNA adduct levels among non-smokers: The role of multiple genetic polymorphisms and nucleotide excision repair phenotype

2012 ◽  
Vol 132 (12) ◽  
pp. 2738-2747 ◽  
Author(s):  
Arash Etemadi ◽  
Farhad Islami ◽  
David H. Phillips ◽  
Roger Godschalk ◽  
Asieh Golozar ◽  
...  
Keyword(s):  
Genetic Polymorphisms ◽  
Nucleotide Excision Repair ◽  
Excision Repair ◽  
Dna Adduct ◽  
Nucleotide Excision

scholarly journals Base pair conformation-dependent excision of benzo[a]pyrene diol epoxide-guanine adducts by human nucleotide excision repair enzymes.

1997 ◽  
Vol 17 (12) ◽  
pp. 7069-7076 ◽  
Author(s):  
M T Hess ◽  
D Gunz ◽  
N Luneva ◽  
N E Geacintov ◽  
H Naegeli
Keyword(s):  
Nucleotide Excision Repair ◽  
Dna Adducts ◽  
Excision Repair ◽  
Dna Conformation ◽  
Repair Processes ◽  
Repair Enzymes ◽  
Diol Epoxide ◽  
Nucleotide Excision ◽  
Guanine Adducts ◽  
Repair Activity

Human nucleotide excision repair processes carcinogen-DNA adducts at highly variable rates, even at adjacent sites along individual genes. Here, we identify conformational determinants of fast or slow repair by testing excision of N2-guanine adducts formed by benzo[a]pyrene diol epoxide (BPDE), a potent and ubiquitous mutagen that induces mainly G x C-->T x A transversions and frameshift deletions. We found that human nucleotide excision repair processes the predominant (+)-trans-BPDE-N2-dG adduct 15 times less efficiently than a standard acetylaminofluorene-C8-dG lesion in the same sequence. No difference was observed between (+)-trans- and (-)-trans-BPDE-N2-dG, but excision was enhanced about 10-fold by changing the adduct configurations to either (+)-cis- or (-)-cis-BPDE-N2-dG. Conversely, excision of (+)-cis- and (-)-cis- but not (+)-trans-BPDE-N2-dG was reduced about 10-fold when the complementary cytosine was replaced by adenine, and excision of these BPDE lesions was essentially abolished when the complementary deoxyribonucleotide was missing. Thus, a set of chemically identical BPDE adducts yielded a greater-than-100-fold range of repair rates, demonstrating that nucleotide excision repair activity is entirely dictated by local DNA conformation. In particular, this unique comparison between structurally highly defined substrates shows that fast excision of BPDE-N2-dG lesions is correlated with displacement of both the modified guanine and its partner base in the complementary strand from their normal intrahelical positions. The very slow excision of carcinogen-DNA adducts located opposite deletion sites reveals a cellular strategy that minimizes the fixation of frameshifts after mutagenic translesion synthesis.

scholarly journals Distant Neighbor Base Sequence Context Effects in Human Nucleotide Excision Repair of a Benzo[a]pyrene-derived DNA Lesion

2010 ◽  
Vol 399 (3) ◽  
pp. 397-409 ◽  
Author(s):  
Yuqin Cai ◽  
Konstantin Kropachev ◽  
Rong Xu ◽  
Yijin Tang ◽  
Marina Kolbanovskii ◽  
...  
Keyword(s):  
Nucleotide Excision Repair ◽  
Context Effects ◽  
Excision Repair ◽  
Base Sequence ◽  
Sequence Context ◽  
Dna Lesion ◽  
Nucleotide Excision ◽  
Distant Neighbor

scholarly journals Cryo-EM structure of TFIIH/Rad4–Rad23–Rad33 in damaged DNA opening in nucleotide excision repair

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Trevor van Eeuwen ◽  
Yoonjung Shim ◽  
Hee Jong Kim ◽  
Tingting Zhao ◽  
Shrabani Basu ◽  
...  
Keyword(s):  
Nucleotide Excision Repair ◽  
Genomic Dna ◽  
Excision Repair ◽  
Dna Lesions ◽  
Dna Adduct ◽  
Dna Unwinding ◽  
General Transcription Factor ◽  
Nucleotide Excision ◽  
Torque Generation ◽  
Transcription Factor Complex

AbstractThe versatile nucleotide excision repair (NER) pathway initiates as the XPC–RAD23B–CETN2 complex first recognizes DNA lesions from the genomic DNA and recruits the general transcription factor complex, TFIIH, for subsequent lesion verification. Here, we present a cryo-EM structure of an NER initiation complex containing Rad4–Rad23-Rad33 (yeast homologue of XPC–RAD23B–CETN2) and 7-subunit coreTFIIH assembled on a carcinogen-DNA adduct lesion at 3.9–9.2 Å resolution. A ~30-bp DNA duplex could be mapped as it straddles between Rad4 and the Ssl2 (XPB) subunit of TFIIH on the 3' and 5' side of the lesion, respectively. The simultaneous binding with Rad4 and TFIIH was permitted by an unwinding of DNA at the lesion. Translocation coupled with torque generation by Ssl2 and Rad4 would extend the DNA unwinding at the lesion and deliver the damaged strand to Rad3 (XPD) in an open form suitable for subsequent lesion scanning and verification.

scholarly journals Adenine-DNA Adduct Derived from the Nitroreduction of 6-Nitrochrysene Is More Resistant to Nucleotide Excision Repair than Guanine-DNA Adducts

2013 ◽  
Vol 26 (11) ◽  
pp. 1746-1754 ◽  
Author(s):  
Jacek Krzeminski ◽  
Konstantin Kropachev ◽  
Dara Reeves ◽  
Aleksandr Kolbanovskiy ◽  
Marina Kolbanovskiy ◽  
...  
Keyword(s):  
Nucleotide Excision Repair ◽  
Dna Adducts ◽  
Excision Repair ◽  
Dna Adduct ◽  
Nucleotide Excision
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