Interaction of G-quadruplex with RecA Protein Studied in Bulk Phase and at the Single-Molecule Level
Interaction of G-quadruplex with RecA Protein Studied in Bulk Phase and at the Single-Molecule Level
复制标题
在本体相和单分子水平上研究 G-四链体与 RecA 蛋白的相互作用
DOI:
10.1021/jp4036277
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发表时间:
2013
期刊:
影响因子:
3.3
通讯作者:
S. K. Kim and T. Majima
中科院分区:
文献类型:
--
作者:
A. Tanaka;J. Choi;S. K. Kim and T. Majima
As in the human genome there are numerous repeat DNA sequences to adopt into non-B DNA structures such as hairpin, triplex, Z-DNA, G-quadruplex, and so on, an understanding of the interaction between DNA repair proteins and a non-B DNA forming sequence is very important. In this regard, the interaction between RecA protein and human telomeric 5′-TAGGG-(TTAGGG)3-TT-3′ sequence and the G-quadruplex formed from this sequence has been investigated in bulk phase and at the single-molecule level. The RecA@ssDNA filament, which is formed by the interaction between RecA protein and a G-rich sequence, was dissociated by the addition of K+ions, and the dissociated G-rich sequence was quickly folded to a G-quadruplex structure, indicating that the G-quadruplex structure is more favorable than the RecA@ssDNA filament in the presence of K+ions. In addition, we demonstrate that the conformation of the G-quadruplex, which is heterogeneous in the absence of RecA, converged to the specific G-quadruplex with one double-chain-reversal loop upon association of RecA protein.