Differences in the Access of Lesions to the Nucleotide Excision Repair Machinery in Nucleosomes

被引：14

作者：

Cai, Yuqin ^{[1
]}

Kropachev, Konstantin ^{[2
]}

Terzidis, Michael A. ^{[3
]}

Masi, Annalisa ^{[3
]}

Chatgilialoglu, Chryssostomos ^{[3
,4
]}

Shafirovich, Vladimir ^{[2
]}

Geacintov, Nicholas E. ^{[2
]}

Broyde, Suse ^{[1
]}

机构：

[1] NYU, Dept Biol, New York, NY 10003 USA

[2] NYU, Dept Chem, New York, NY 10003 USA

[3] Ist Sintesi Organ & Fotoreattivita, Consiglio Nazl Ric, I-40129 Bologna, Italy

[4] Natl Ctr Sci Res Demokritos, Inst Nanosci & Nanotechnol, Athens 15341, Greece

来源：

BIOCHEMISTRY | 2015年 / 54卷 / 27期

基金：

美国国家科学基金会;

关键词：

DNA LESIONS; SOLUTION CONFORMATION; UV PHOTOPRODUCT; DAMAGE; CHROMATIN; (5'S)-8,5'-CYCLO-2'-DEOXYGUANOSINE; STABILITY; PATHWAY; ENZYMES; DUPLEX;

D O I：

10.1021/acs.biochem.5b00564

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

In nucleosomes, the access of DNA lesions to nucleotide excision repair is hindered by histone proteins. However, evidence that the nature of the DNA lesions may play a role in facilitating access is emerging, but these phenomena are not well-understood. We have used molecular dynamics simulations to elucidate the structural, dynamic, and energetic properties of the R and S 5'-8-cydo-2'-dG and the (+)-cis-anti-B[a]P-dG lesions in a nudeosome. Our results show that the (+)-cis-anti-B [a]P-dG adduct is more dynamic and more destabilizing than the smaller and more constrained 5',8-cyclo-2'-dG lesions, suggesting more facile access to the more bulky (+)-cis-anti-B [a]P-dG lesion.

引用

页码：4181 / 4185

页数：5

共 41 条

[1] The Protein Data Bank [J].