Genetic Control or Repair and Adaptive Response to Low-Level DNA Damage
- Brandeis University
Research was focused on how a single double-strand break - a model of low-dose ionizing radiation-induced DNA damage - could be studied in a simple model system, budding yeast. Breaks were induced in several different ways. We used the site-specific HO endonuclease to create a single DSB in all cells of the population so that its fate could be extensively analyzed genetically and molecularly. We also used two heterologous systems, the plant DS element and the Rag1/Rag2 proteins, to generate different types of DSBs, these containing hairpin ends that needed to be cleaved open before end-joining could take place. All three approaches yielded important new findings. We also extended our analysis of the Mre11 protein that plays key roles in both NHEJ and in homologous recombination. Finally we analyzed the poorly understood recombination events that were independent of the key recombination protein, Rad52. This line of inquiry was strongly motivated by the fact that vertebrate cells do not rely strongly on Rad52 for homologous recombination, so that some clues about alternative mechanisms could be gained by understanding how Rad52-independent recombination occurred. We found that the Mre11 complex was the most important element in Rad52-independent recombination.
- Research Organization:
- Brandeis University
- Sponsoring Organization:
- USDOE
- DOE Contract Number:
- FG02-01ER63229
- OSTI ID:
- 965273
- Report Number(s):
- DOE/ER/63229
- Country of Publication:
- United States
- Language:
- English
Similar Records
The C-terminal region of Rad52 is essential for Rad52 nuclear and nucleolar localization, and accumulation at DNA damage sites immediately after irradiation
Crystal structure of the V(D)J recombinase RAG1–RAG2
Microhomology-mediated end joining is activated in irradiated human cells due to phosphorylation-dependent formation of the XRCC1 repair complex
Journal Article
·
Fri May 31 00:00:00 EDT 2013
· Biochemical and Biophysical Research Communications
·
OSTI ID:22239609
Crystal structure of the V(D)J recombinase RAG1–RAG2
Journal Article
·
Tue Feb 17 19:00:00 EST 2015
· Nature (London)
·
OSTI ID:1247328
Microhomology-mediated end joining is activated in irradiated human cells due to phosphorylation-dependent formation of the XRCC1 repair complex
Journal Article
·
Sun Dec 18 19:00:00 EST 2016
· Nucleic Acids Research
·
OSTI ID:1625550