Analysis of DNA damage repair by Cell Journal of Zhejiang University
Maintaining the stability of genomic DNA is essential for cell survival and tumor suppression. Scientists at the Life Science Research Institute of Zhejiang University have studied an important complex in the DNA repair mechanism and explained the structural basis for the assembly and function of the complex. The article was published in the Cell Reports magazine of Cell on March 13.
The integrity of the cell genome continues to be challenged by a variety of internal and external factors, such as replication fork collapse, oxidative stress, and ionizing radiation. These factors cause damage to the DNA, and the cell is constantly repairing. If such repair fails, the DNA will undergo a double-strand break (DSB). DSB will continue to accumulate with age. It can be said that our health depends largely on the ability of cells to detect and repair DNA damage.
DSB is highly toxic. When the broken chains try to connect again, because there is no template to follow, it is easy to cause chromosome translocation and genome rearrangement. The defects repaired by DSB will not only make the genome unstable, but also cause a variety of diseases, including developmental disorders, premature aging and cancer.
Professor Huang Jun of Zhejiang University took the lead in purifying a new DNA single-strand binding protein complex SOSS (including subunits SOSS-A, SOSS-B1 / B2 and SOSS-C). Now he and Professor Song Haiwei jointly lead the research team to show people the structural basis for the assembly and function of the SOSS1 complex.
The SOSS1 complex is composed of SOSSA, SOSSB1 and SOSSC, and is responsible for sensing single-stranded DNA (ssDNA) and promoting the repair of DNA double-strand breaks. So far, it is unclear the specific assembly process of SOSS1, and the detailed mechanism of recognition of ssDNA.
The researchers found through crystal structure analysis that the N-terminal of SOSSA is a scaffold assembled by SOSS1, which is combined with SOSSB1 and SOSSC. In addition, SOSSB1 interacts with SOSSAN and ssDNA through two different faces. Studies have shown that SOSS1's recognition of ssDNA is completely mediated by SOSSB1, while SOSSC and SOSSAN are not so important for ssDNA binding.
These results reveal the structural basis of SOSS1 assembly, and also provide a framework for future research, which helps to further understand the control mechanism of SOSS1 complex recognition ssDNA.
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