AI Article Synopsis
- The study investigates how DNA double-strand breaks (DSBs) are repaired in yeast using proteins from the RAD52 epistasis group, focusing on the order in which key proteins are recruited to the DSB.
- Using chromatin immunoprecipitation (ChIP), the researchers found that Rad51p is the first protein to bind, followed by a coordinated assembly of Rad52p, Rad54p, and Rad55p that supports Rad51p function.
- The results show that these proteins not only help form a stable nucleoprotein filament crucial for DNA repair but also interact with homologous donor sequences during the process of strand invasion.
Article Abstract
Repair of DNA double-strand breaks (DSBs) by homologous recombination requires members of the RAD52 epistasis group. Here we use chromatin immunoprecipitation (ChIP) to examine the temporal order of recruitment of Rad51p, Rad52p, Rad54p, Rad55p, and RPA to a single, induced DSB in yeast. Our results suggest a sequential, interdependent assembly of Rad proteins adjacent to the DSB initiated by binding of Rad51p. ChIP time courses from various mutant strains and additional biochemical studies suggest that Rad52p, Rad55p, and Rad54p each help promote the formation and/or stabilization of the Rad51p nucleoprotein filament. We also find that all four Rad proteins associate with homologous donor sequences during strand invasion. These studies provide a near comprehensive view of the molecular events required for the in vivo assembly of a functional Rad51p presynaptic filament.
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| http://dx.doi.org/10.1016/s1097-2765(03)00242-9 | DOI Listing |
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