Interaction of Nucleotide Excision Repair Proteins with DNA Containing Bulky Lesion and Aapurinic/Aapyrimidinic Site

被引:3
|
作者
Skosareva, L. V. [1 ]
Lebedeva, N. A. [1 ]
Rechkunova, N. I. [1 ]
Maltseva, E. A. [1 ]
Pestryakov, P. E. [1 ]
Lavrik, O. I. [1 ]
机构
[1] Inst Chem Biol & Fundamental Med, Novosibirsk 630090, Russia
基金
俄罗斯基础研究基金会;
关键词
protein factors of nucleotide excision repair; bulky lesion; apurinic/apyrimidinic site; affinity labeling; DNA-protein complexes; GROUP-C PROTEIN; GROUP-A PROTEIN; DAMAGED DNA; ABASIC SITES; QUALITY-CONTROL; CROSS-LINKING; RECOGNITION; BINDING; BASE; MECHANISM;
D O I
10.1134/S0006297912050136
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
The interaction of nucleotide excision repair (NER) proteins (XPC-HR23b, RPA, and XPA) with 48-mer DNA duplexes containing the bulky lesion-mimicking fluorescein-substituted derivative of dUMP (5-{3-[6-(carboxyamidofluoresceinyl)amidocapromoyl]allyl}-2'-deoxyuridine-5'-monophosphate) in a cluster with a lesion of another type (apurinic/apyrimidinic (AP) site) has been studied. It is shown that XPC-HR23b is modified to a greater extent by the DNA duplex containing an AP site opposite nucleotide adjacent to the fluorescein residue than by DNA containing an AP site shifted to the 3'-or 5'-end of the DNA strand. The efficiency of XPA modification by DNA duplexes containing both AP site and fluorescein residue is higher than that by DNA lacking the bulky lesion; the modification pattern in this case depends on the AP site position. In accordance with its major function, RPA interacts more efficiently with single-stranded DNA than with DNA duplexes, including those bearing bulky lesions. The observed interaction between the proteins involved in nucleotide excision repair and DNA structures containing a bulky lesion processed by NER and the AP site repaired via base excision repair may be significant for both these repair pathways in cells and requires the specific sequence of repair of clustered DNA lesions.
引用
收藏
页码:524 / 531
页数:8
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