The phosphorylated trimeric SOSS1 complex and RNA polymerase II
trigger liquid-liquid phase separation at double-strand breaks

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The phosphorylated trimeric SOSS1 complex and RNA polymerase II trigger liquid-liquid phase ...

Přehled o publikaci

J 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.

Základní údaje

Originální název

The phosphorylated trimeric SOSS1 complex and RNA polymerase II trigger liquid-liquid phase separation at double-strand breaks

Autoři

LONG, Qilin; Marek ŠEBESTA (703 Slovensko, garant, domácí); Kateřina ŠEDOVÁ (203 Česká republika, domácí); Vojtěch HALUZA (203 Česká republika, domácí); Adele ALAGIA; Zhichao LIU; Richard ŠTEFL (203 Česká republika, domácí) a Monika GULLEROVA

Vydání

CELL REPORTS, UNITED STATES, CELL PRESS, 2023, 2211-1247

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Kód RIV

RIV/00216224:14740/23:00133166

Organizace

Středoevropský technologický institut – Masarykova univerzita – Repozitář

DOI

http://dx.doi.org/10.1016/j.celrep.2023.113489

UT WoS

001127113200001

EID Scopus

2-s2.0-85178153659

Klíčová slova anglicky

c-Abl kinase; CP: Molecular biology; DNA damage; DNA:RNA hybrids; hSSB1; LLPS; phase-separation; phosphorylation; R-loops; RNA polymerase II; SOSS1 complex

Návaznosti

EF18_046/0015974, projekt VaV. GM21-10464M, projekt VaV. 649030, interní kód Repo. CIISB III, velká výzkumná infrastruktura. Czech-BioImaging III, velká výzkumná infrastruktura. e-INFRA CZ II, velká výzkumná infrastruktura.

Změněno: 8. 1. 2025 00:50, RNDr. Daniel Jakubík

Anotace

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.

Přiložené soubory

https://is.muni.cz/publication/2364700/1-s2.0-S2211124723015012-main.pdf

Citovat

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. CELL REPORTS. UNITED STATES: CELL PRESS, 2023, roč. 42, č. 12, s. 1-25. ISSN 2211-1247. Dostupné z: https://dx.doi.org/10.1016/j.celrep.2023.113489.

@article{63506,
   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_location = {UNITED STATES},
   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  - 63506
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  - CELL PRESS
SN  - 2211-1247
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}. UNITED STATES: CELL PRESS, 2023, roč.~42, č.~12, s.~1-25. ISSN~2211-1247. Dostupné z: https://dx.doi.org/10.1016/j.celrep.2023.113489.