Plasticity of the Mre11-Rad50-Xrs2-Sae2 nuclease ensemble in the processing of DNA-bound obstacles [Research Communications]
Wang, W., Daley, J. M., Kwon, Y., Krasner, D. S., Sung, P.
Cold Spring Harbor Laboratory Press
Published 2018
Cold Spring Harbor Laboratory Press
Published 2018
| Publication Date: |
2018-01-20
|
|---|---|
| Publisher: |
Cold Spring Harbor Laboratory Press
|
| Print ISSN: |
0890-9369
|
| Topics: |
Biology
|
| Published by: |
| _version_ | 1836398757571198977 |
|---|---|
| autor | Wang, W., Daley, J. M., Kwon, Y., Krasner, D. S., Sung, P. |
| beschreibung | The budding yeast Mre11–Rad50–Xrs2 (MRX) complex and Sae2 function together in DNA end resection during homologous recombination. Here we show that the Ku complex shields DNA ends from exonucleolytic digestion but facilitates endonucleolytic scission by MRX with a dependence on ATP and Sae2. The incision site is enlarged into a DNA gap via the exonuclease activity of MRX, which is stimulated by Sae2 without ATP being present. RPA renders a partially resected or palindromic DNA structure susceptible to MRX–Sae2, and internal protein blocks also trigger DNA cleavage. We present models for how MRX–Sae2 creates entry sites for the long-range resection machinery. |
| citation_standardnr | 6142629 |
| datenlieferant | ipn_articles |
| feed_id | 1644 |
| feed_publisher | Cold Spring Harbor Laboratory Press |
| feed_publisher_url | http://www.cshlpress.com/ |
| insertion_date | 2018-01-20 |
| journalissn | 0890-9369 |
| publikationsjahr_anzeige | 2018 |
| publikationsjahr_facette | 2018 |
| publikationsjahr_intervall | 7984:2015-2019 |
| publikationsjahr_sort | 2018 |
| publisher | Cold Spring Harbor Laboratory Press |
| quelle | Genes & Development |
| relation | http://genesdev.cshlp.org/cgi/content/short/31/23-24/2331?rss=1 |
| search_space | articles |
| shingle_author_1 | Wang, W., Daley, J. M., Kwon, Y., Krasner, D. S., Sung, P. |
| shingle_author_2 | Wang, W., Daley, J. M., Kwon, Y., Krasner, D. S., Sung, P. |
| shingle_author_3 | Wang, W., Daley, J. M., Kwon, Y., Krasner, D. S., Sung, P. |
| shingle_author_4 | Wang, W., Daley, J. M., Kwon, Y., Krasner, D. S., Sung, P. |
| shingle_catch_all_1 | Plasticity of the Mre11-Rad50-Xrs2-Sae2 nuclease ensemble in the processing of DNA-bound obstacles [Research Communications] The budding yeast Mre11–Rad50–Xrs2 (MRX) complex and Sae2 function together in DNA end resection during homologous recombination. Here we show that the Ku complex shields DNA ends from exonucleolytic digestion but facilitates endonucleolytic scission by MRX with a dependence on ATP and Sae2. The incision site is enlarged into a DNA gap via the exonuclease activity of MRX, which is stimulated by Sae2 without ATP being present. RPA renders a partially resected or palindromic DNA structure susceptible to MRX–Sae2, and internal protein blocks also trigger DNA cleavage. We present models for how MRX–Sae2 creates entry sites for the long-range resection machinery. Wang, W., Daley, J. M., Kwon, Y., Krasner, D. S., Sung, P. Cold Spring Harbor Laboratory Press 0890-9369 08909369 |
| shingle_catch_all_2 | Plasticity of the Mre11-Rad50-Xrs2-Sae2 nuclease ensemble in the processing of DNA-bound obstacles [Research Communications] The budding yeast Mre11–Rad50–Xrs2 (MRX) complex and Sae2 function together in DNA end resection during homologous recombination. Here we show that the Ku complex shields DNA ends from exonucleolytic digestion but facilitates endonucleolytic scission by MRX with a dependence on ATP and Sae2. The incision site is enlarged into a DNA gap via the exonuclease activity of MRX, which is stimulated by Sae2 without ATP being present. RPA renders a partially resected or palindromic DNA structure susceptible to MRX–Sae2, and internal protein blocks also trigger DNA cleavage. We present models for how MRX–Sae2 creates entry sites for the long-range resection machinery. Wang, W., Daley, J. M., Kwon, Y., Krasner, D. S., Sung, P. Cold Spring Harbor Laboratory Press 0890-9369 08909369 |
| shingle_catch_all_3 | Plasticity of the Mre11-Rad50-Xrs2-Sae2 nuclease ensemble in the processing of DNA-bound obstacles [Research Communications] The budding yeast Mre11–Rad50–Xrs2 (MRX) complex and Sae2 function together in DNA end resection during homologous recombination. Here we show that the Ku complex shields DNA ends from exonucleolytic digestion but facilitates endonucleolytic scission by MRX with a dependence on ATP and Sae2. The incision site is enlarged into a DNA gap via the exonuclease activity of MRX, which is stimulated by Sae2 without ATP being present. RPA renders a partially resected or palindromic DNA structure susceptible to MRX–Sae2, and internal protein blocks also trigger DNA cleavage. We present models for how MRX–Sae2 creates entry sites for the long-range resection machinery. Wang, W., Daley, J. M., Kwon, Y., Krasner, D. S., Sung, P. Cold Spring Harbor Laboratory Press 0890-9369 08909369 |
| shingle_catch_all_4 | Plasticity of the Mre11-Rad50-Xrs2-Sae2 nuclease ensemble in the processing of DNA-bound obstacles [Research Communications] The budding yeast Mre11–Rad50–Xrs2 (MRX) complex and Sae2 function together in DNA end resection during homologous recombination. Here we show that the Ku complex shields DNA ends from exonucleolytic digestion but facilitates endonucleolytic scission by MRX with a dependence on ATP and Sae2. The incision site is enlarged into a DNA gap via the exonuclease activity of MRX, which is stimulated by Sae2 without ATP being present. RPA renders a partially resected or palindromic DNA structure susceptible to MRX–Sae2, and internal protein blocks also trigger DNA cleavage. We present models for how MRX–Sae2 creates entry sites for the long-range resection machinery. Wang, W., Daley, J. M., Kwon, Y., Krasner, D. S., Sung, P. Cold Spring Harbor Laboratory Press 0890-9369 08909369 |
| shingle_title_1 | Plasticity of the Mre11-Rad50-Xrs2-Sae2 nuclease ensemble in the processing of DNA-bound obstacles [Research Communications] |
| shingle_title_2 | Plasticity of the Mre11-Rad50-Xrs2-Sae2 nuclease ensemble in the processing of DNA-bound obstacles [Research Communications] |
| shingle_title_3 | Plasticity of the Mre11-Rad50-Xrs2-Sae2 nuclease ensemble in the processing of DNA-bound obstacles [Research Communications] |
| shingle_title_4 | Plasticity of the Mre11-Rad50-Xrs2-Sae2 nuclease ensemble in the processing of DNA-bound obstacles [Research Communications] |
| timestamp | 2025-06-30T23:32:09.774Z |
| titel | Plasticity of the Mre11-Rad50-Xrs2-Sae2 nuclease ensemble in the processing of DNA-bound obstacles [Research Communications] |
| titel_suche | Plasticity of the Mre11-Rad50-Xrs2-Sae2 nuclease ensemble in the processing of DNA-bound obstacles [Research Communications] |
| topic | W |
| uid | ipn_articles_6142629 |