The N-terminal domain of Escherichia coli RecA have multiple functions in promoting homologous recombination.
The N-terminal domain of Escherichia coli RecA have multiple functions in promoting homologous recombination.
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DOI：
10.1186/1423-0127-16-37
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发表时间：
2009-04-01
影响因子：
11
通讯作者：
Wang TF
中科院分区：
文献类型：
--
作者：
Lee CD;Wang TF
Escherichia coli RecA mediates homologous recombination, a process essential to maintaining genome integrity. In the presence of ATP, RecA proteins bind a single-stranded DNA (ssDNA) to form a RecA-ssDNA presynaptic nucleoprotein filament that captures donor double-stranded DNA (dsDNA), searches for homology, and then catalyzes the strand exchange between ssDNA and dsDNA to produce a new heteroduplex DNA. Based upon a recently reported crystal structure of the RecA-ssDNA nucleoprotein filament, we carried out structural and functional studies of the N-terminal domain (NTD) of the RecA protein. The RecA NTD was thought to be required for monomer-monomer interaction. Here we report that it has two other distinct roles in promoting homologous recombination. It first facilitates the formation of a RecA-ssDNA presynaptic nucleoprotein filament by converting ATP to an ADP-Pi intermediate. Then, once the RecA-ssDNA presynaptic nucleoprotein filament is stably assembled in the presence of ATPγS, the NTD is required to capture donor dsDNA. Our results also suggest that the second function of NTD may be similar to that of Arg243 and Lys245, which were implicated earlier as binding sites of donor dsDNA. A two-step model is proposed to explain how a RecA-ssDNA presynaptic nucleoprotein filament interacts with donor dsDNA.
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影响因子：
3.7
作者：
Chen LT;Ko TP;Chang YW;Lin KA;Wang AH;Wang TF
通讯作者：
Wang TF
影响因子：
8
作者：
Lee, Chien-Der;Sun, Hui-Chien;Wang, Ting-Fang
通讯作者：
Wang, Ting-Fang
影响因子：
5.6
作者：
Aihara, H;Ito, Y;Shibata, T
通讯作者：
Shibata, T
影响因子：
3.9
作者：
Kurumizaka, H;Ikawa, S;Shibata, T
通讯作者：
Shibata, T
影响因子：
4.8
作者：
Kurumizaka, H;Aihara, H;Shibata, T
通讯作者：
Shibata, T