Přehled o publikaci
2024
The phosphorylated trimeric SOSS1 complex and RNA polymerase II trigger liquid‐liquid phase separation at double‐strand breaks
LONG, Qilin, Kateřina ŠEDOVÁ, Vojtěch HALUZA, Adele ALAGIA, Zhichao LIU et. al.Basic information
Original name
The phosphorylated trimeric SOSS1 complex and RNA polymerase II trigger liquid‐liquid phase separation at double‐strand breaks
Authors
LONG, Qilin, Kateřina ŠEDOVÁ, Vojtěch HALUZA, Adele ALAGIA, Zhichao LIU, Richard ŠTEFL, Monika GULLEROVA and Marek ŠEBESTA
Edition
29th Annual International Conference RNA 2024, Edinburg, 2024, 2024
Other information
Language
English
Type of outcome
Presentations at conferences
Country of publisher
United Kingdom of Great Britain and Northern Ireland
Confidentiality degree
is not subject to a state or trade secret
References:
Organization
Středoevropský technologický institut – Repository – Repository
Keywords in English
RNA polymerase II; DSBs; CTD; trimeric SOSS1 complex; R‐loops
Links
EH22_008/0004575, research and development project.
Changed: 11/2/2025 00:50, RNDr. Daniel Jakubík
Abstract
V originále
Double‐strand breaks (DSBs) are the most severe type of DNA damage. Previously, we demonstrated that RNA polymerase II (RNAPII) phosphorylated at the tyrosine 1 (Y1P) residue of its C‐terminal domain (CTD) generates RNAs at DSBs. However, the regulation of transcription at DSBs remains enigmatic. Here, we show that the damage‐activated tyrosine kinase c‐Abl phosphorylates hSSB1, enabling its interaction with Y1P RNAPII at DSBs. Furthermore, the trimeric SOSS1 complex, consisting of hSSB1, INTS3, and c9orf80, binds to Y1P RNAPII in response to DNA damage in an R‐loop‐dependent manner. Specifically, hSSB1, as a part of the trimeric SOSS1 complex, exhibits a strong affinity for R‐loops, even in the presence of replication protein A (RPA). Our in vitro and in vivo data reveal that the SOSS1 complex and RNAPII form dynamic liquid‐like repair compartments at DSBs. Depletion of the SOSS1 complex impairs DNA repair, underscoring its biological role in the R‐loop‐dependent DNA damage response.
