The N-terminal domain of <it>Escherichia coli </it>RecA have multiple functions in promoting homologous recombination
<p>Abstract</p> <p><it>Escherichia coli </it>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 tha...
| Main Authors: | , |
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| Format: | Article |
| Language: | English |
| Published: |
BMC
2009-04-01
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| Series: | Journal of Biomedical Science |
| Online Access: | http://www.jbiomedsci.com/content/16/1/37 |
| _version_ | 1828420064009781248 |
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| author | Wang Ting-Fang Lee Chien-Der |
| author_facet | Wang Ting-Fang Lee Chien-Der |
| author_sort | Wang Ting-Fang |
| collection | DOAJ |
| description | <p>Abstract</p> <p><it>Escherichia coli </it>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.</p> |
| first_indexed | 2024-12-10T15:05:21Z |
| format | Article |
| id | doaj.art-6138284a05c7476e8d142802754f1d4c |
| institution | Directory Open Access Journal |
| issn | 1021-7770 1423-0127 |
| language | English |
| last_indexed | 2024-12-10T15:05:21Z |
| publishDate | 2009-04-01 |
| publisher | BMC |
| record_format | Article |
| series | Journal of Biomedical Science |
| spelling | doaj.art-6138284a05c7476e8d142802754f1d4c2022-12-22T01:44:04ZengBMCJournal of Biomedical Science1021-77701423-01272009-04-011613710.1186/1423-0127-16-37The N-terminal domain of <it>Escherichia coli </it>RecA have multiple functions in promoting homologous recombinationWang Ting-FangLee Chien-Der<p>Abstract</p> <p><it>Escherichia coli </it>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.</p>http://www.jbiomedsci.com/content/16/1/37 |
| spellingShingle | Wang Ting-Fang Lee Chien-Der The N-terminal domain of <it>Escherichia coli </it>RecA have multiple functions in promoting homologous recombination Journal of Biomedical Science |
| title | The N-terminal domain of <it>Escherichia coli </it>RecA have multiple functions in promoting homologous recombination |
| title_full | The N-terminal domain of <it>Escherichia coli </it>RecA have multiple functions in promoting homologous recombination |
| title_fullStr | The N-terminal domain of <it>Escherichia coli </it>RecA have multiple functions in promoting homologous recombination |
| title_full_unstemmed | The N-terminal domain of <it>Escherichia coli </it>RecA have multiple functions in promoting homologous recombination |
| title_short | The N-terminal domain of <it>Escherichia coli </it>RecA have multiple functions in promoting homologous recombination |
| title_sort | n terminal domain of it escherichia coli it reca have multiple functions in promoting homologous recombination |
| url | http://www.jbiomedsci.com/content/16/1/37 |
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