Interaction of G-Quadruplex with RecA Protein Studied in Bulk Phase and at the Single-Molecule Level

Title
Interaction of G-Quadruplex with RecA Protein Studied in Bulk Phase and at the Single-Molecule Level
Author(s)
김석규Atsushi Tanaka[Atsushi Tanaka]Jungkweon Choi[Jungkweon Choi]Tetsuro Majima[Tetsuro Majima]
Keywords
NON-B DNA; FLUORESCENCE CORRELATION SPECTROSCOPY; REAL-TIME OBSERVATION; ESCHERICHIA-COLI; HOMOLOGOUS RECOMBINATION; FILAMENT DYNAMICS; HUMAN-DISEASE; MECHANISM; BINDING; RESOLUTION
Issue Date
201306
Publisher
AMER CHEMICAL SOC
Citation
JOURNAL OF PHYSICAL CHEMISTRY B, v.117, no.22, pp.6711 - 6717
Abstract
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.
URI
http://hdl.handle.net/YU.REPOSITORY/29964http://dx.doi.org/10.1021/jp4036277
ISSN
1520-6106
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이과대학 > 화학생화학부 > Articles
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