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@article{2364700,
author = {Long, Qilin and Šebesta, Marek and Šedová, Kateřina and Haluza, Vojtěch and Alagia, Adele and Liu, Zhichao and Štefl, Richard and Gullerova, Monika},
article_number = {12},
doi = {http://dx.doi.org/10.1016/j.celrep.2023.113489},
keywords = {c-Abl kinase; CP: Molecular biology; DNA damage; DNA:RNA hybrids; hSSB1; LLPS; phase-separation; phosphorylation; R-loops; RNA polymerase II; SOSS1 complex},
language = {eng},
issn = {2211-1247},
journal = {Cell Reports},
title = {The phosphorylated trimeric SOSS1 complex and RNA polymerase II trigger liquid-liquid phase separation at double-strand breaks},
url = {https://www.sciencedirect.com/science/article/pii/S2211124723015012},
volume = {42},
year = {2023}
}
TY - JOUR
ID - 2364700
AU - Long, Qilin - Šebesta, Marek - Šedová, Kateřina - Haluza, Vojtěch - Alagia, Adele - Liu, Zhichao - Štefl, Richard - Gullerova, Monika
PY - 2023
TI - The phosphorylated trimeric SOSS1 complex and RNA polymerase II trigger liquid-liquid phase separation at double-strand breaks
JF - Cell Reports
VL - 42
IS - 12
SP - 1-25
EP - 1-25
PB - Elsevier
SN - 22111247
KW - c-Abl kinase
KW - CP: Molecular biology
KW - DNA damage
KW - DNA:RNA hybrids
KW - hSSB1
KW - LLPS
KW - phase-separation
KW - phosphorylation
KW - R-loops
KW - RNA polymerase II
KW - SOSS1 complex
UR - https://www.sciencedirect.com/science/article/pii/S2211124723015012
N2 - 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.
ER -
LONG, Qilin, Marek ŠEBESTA, Kateřina ŠEDOVÁ, Vojtěch HALUZA, Adele ALAGIA, Zhichao LIU, Richard ŠTEFL a Monika GULLEROVA. The phosphorylated trimeric SOSS1 complex and RNA polymerase II trigger liquid-liquid phase separation at double-strand breaks. \textit{Cell Reports}. Elsevier, 2023, roč.~42, č.~12, s.~1-25. ISSN~2211-1247. Dostupné z: https://dx.doi.org/10.1016/j.celrep.2023.113489.
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