Abstract:
:RNA molecules have been found to play important roles in DNA double-strand break (DSB) repair, but the exact underlying mechanism remains unclear. Here, we aimed to clarify the function of RNase L, an important ribonuclease in the immune system of vertebrates, in DSB repair. Knockdown of RNase L reduces cell survival after induction of DSBs by ionizing radiation or camptothecin and causes a significant decrease in DSB repair, as evidenced by an increase in the extent of phosphorylation of histone H2AX on Ser139 (γH2AX) and γH2AX nuclear foci formation. Thus, our findings indicate that RNase L interacts with the core factors involved in DNA end joining, such as XRCC4 and Lig4, and facilitates DSB repair through the nonhomologous end-joining pathway.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Zhong Y,Pan B,Zhu J,Fu H,Zheng Xdoi
10.1002/1873-3468.13426subject
Has Abstractpub_date
2019-06-01 00:00:00pages
1190-1200issue
11eissn
0014-5793issn
1873-3468journal_volume
593pub_type
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