My note on paper: RNF8 Ubiquitylates Histones at DNA Double-Strand Breaks and Promotes Assembly of Repair Proteins

Paper: RNF8 Ubiquitylates Histones at DNA Double-Strand Breaks and Promotes Assembly of Repair Proteins
(http://dx.doi.org/10.1016/j.cell.2007.09.040)

Conclusion for my own study on RING-finger protein in DNA repair;

General overview:
DNA repair is important to maintain genome integrity

Research question:
The mechanisms of proteins retention at db strand break is not clear -- that is why they want to study how the dbDNA is recognized

Results:
1. RNF8 is recruited to the DSB via the interaction between FHA domain at N-terminal vs P-MDC1
2. Increase in DSB Ubiquitinylation (when knock down-RNF8 or disrupt the RING/FHA domain reduce DSB associated ubiquitinylation)
3. Recruitment of 53BP1 and BRCA1 (when knock down-RNF8 or disrupt the RING/FHA domain reduce the retention of those two proteins)
4. RNF8 is important for IR-induced damage
5. RNF8 protect genome integrity by issuing chromatin that franks the DNA db strand break

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Remarks:
Cell line using in this study -- U2OS osteosarcoma cells (easy to handle and there are some studies investigate on DNA repair)


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