Přehled o publikaci
2023
The phosphorylated trimeric SOSS1 complex and RNA polymerase II trigger liquid-liquid phase separation at double-strand breaks
LONG, Qilin; Marek ŠEBESTA; Kateřina ŠEDOVÁ; Vojtěch HALUZA; Adele ALAGIA 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; Marek ŠEBESTA; Kateřina ŠEDOVÁ; Vojtěch HALUZA; Adele ALAGIA; Zhichao LIU; Richard ŠTEFL and Monika GULLEROVA
Edition
CELL REPORTS, UNITED STATES, CELL PRESS, 2023, 2211-1247
Other information
Language
English
Type of outcome
Article in a journal
Country of publisher
United States of America
Confidentiality degree
is not subject to a state or trade secret
References:
Marked to be transferred to RIV
Yes
RIV identification code
RIV/00216224:14740/23:00133166
Organization
Středoevropský technologický institut – Repository – Repository
UT WoS
EID Scopus
Keywords in English
c-Abl kinase; CP: Molecular biology; DNA damage; DNA:RNA hybrids; hSSB1; LLPS; phase-separation; phosphorylation; R-loops; RNA polymerase II; SOSS1 complex
Links
EF18_046/0015974, research and development project. GM21-10464M, research and development project. 649030, interní kód Repo. CIISB III, large research infrastructures. Czech-BioImaging III, large research infrastructures. e-INFRA CZ II, large research infrastructures.
Changed: 8/1/2025 00:50, RNDr. Daniel Jakubík
Abstract
In the original language
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.
