DSS1 interacts with and stimulates RAD52 to promote the repair
of DSBs

J 2020

DSS1 interacts with and stimulates RAD52 to promote the repair of DSBs

ŠTEFANOVIE, Barbora, Sarah R. HENGEL, Jarmila MLČOUŠKOVÁ, Jana PROCHAZKOVA, Mário ŠPÍREK et. al.

Basic information

Original name

DSS1 interacts with and stimulates RAD52 to promote the repair of DSBs

Authors

ŠTEFANOVIE, Barbora (703 Slovakia, belonging to the institution), Sarah R. HENGEL, Jarmila MLČOUŠKOVÁ (203 Czech Republic, belonging to the institution), Jana PROCHAZKOVA, Mário ŠPÍREK (703 Slovakia, belonging to the institution), Fedor NIKULENKOV, Daniel NĚMEČEK (203 Czech Republic, belonging to the institution), Brandon G. KOCH, Fletcher E. BAIN, Liping YU, Maria SPIES and Lumír KREJČÍ (203 Czech Republic, guarantor, belonging to the institution)

Edition

Nucleic Acids Research, Oxford, Oxford University Press, 2020, 0305-1048

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10608 Biochemistry and molecular biology

Country of publisher

United Kingdom of Great Britain and Northern Ireland

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Impact factor

Impact factor: 16.971

RIV identification code

RIV/00216224:14310/20:00114494

Organization unit

Faculty of Science

DOI

http://dx.doi.org/10.1093/nar/gkz1052

UT WoS

000518532100019

Keywords in English

Genome integrity; repair and replication

Abstract

V originále

The proper repair of deleterious DNA lesions such as double strand breaks prevents genomic instability and carcinogenesis. In yeast, the Rad52 protein mediates DSB repair via homologous recombination. In mammalian cells, despite the presence of the RAD52 protein, the tumour suppressor protein BRCA2 acts as the predominant mediator during homologous recombination. For decades, it has been believed that the RAD52 protein played only a back-up role in the repair of DSBs performing an error-prone single strand annealing (SSA). Recent studies have identified several new functions of the RAD52 protein and have drawn attention to its important role in genome maintenance. Here, we show that RAD52 activities are enhanced by interacting with a small and highly acidic protein called DSS1. Binding of DSS1 to RAD52 changes the RAD52 oligomeric conformation, modulates its DNA binding properties, stimulates SSA activity and promotes strand invasion. Our work introduces for the first time RAD52 as another interacting partner of DSS1 and shows that both proteins are important players in the SSA and BIR pathways of DSB repair.

Links

GA17-17720S, research and development project

Name: Vnitřní vlastnosti RAD51 vlákna a jeho biologické regulace

Investor: Czech Science Foundation

206292/E/17/Z, interní kód MU

Name: Mechanics and execution of homologous recombination - biophysics to the organism

Investor: Wellcome Trust

90043, large research infrastructures

Name: CIISB

Citovat

ŠTEFANOVIE, Barbora, Sarah R. HENGEL, Jarmila MLČOUŠKOVÁ, Jana PROCHAZKOVA, Mário ŠPÍREK, Fedor NIKULENKOV, Daniel NĚMEČEK, Brandon G. KOCH, Fletcher E. BAIN, Liping YU, Maria SPIES and Lumír KREJČÍ. DSS1 interacts with and stimulates RAD52 to promote the repair of DSBs. Nucleic Acids Research. Oxford: Oxford University Press, 2020, vol. 48, No 2, p. 694-708. ISSN 0305-1048. Available from: https://dx.doi.org/10.1093/nar/gkz1052.

@article{1698276,
   author = {Štefanovie, Barbora and Hengel, Sarah R. and Mlčoušková, Jarmila and Prochazkova, Jana and Špírek, Mário and Nikulenkov, Fedor and Němeček, Daniel and Koch, Brandon G. and Bain, Fletcher E. and Yu, Liping and Spies, Maria and Krejčí, Lumír},
   article_location = {Oxford},
   article_number = {2},
   doi = {http://dx.doi.org/10.1093/nar/gkz1052},
   keywords = {Genome integrity; repair and replication},
   language = {eng},
   issn = {0305-1048},
   journal = {Nucleic Acids Research},
   title = {DSS1 interacts with and stimulates RAD52 to promote the repair of DSBs},
   url = {https://doi.org/10.1093/nar/gkz1052},
   volume = {48},
   year = {2020}
}

TY  - JOUR
ID  - 1698276
AU  - Štefanovie, Barbora - Hengel, Sarah R. - Mlčoušková, Jarmila - Prochazkova, Jana - Špírek, Mário - Nikulenkov, Fedor - Němeček, Daniel - Koch, Brandon G. - Bain, Fletcher E. - Yu, Liping - Spies, Maria - Krejčí, Lumír
PY  - 2020
TI  - DSS1 interacts with and stimulates RAD52 to promote the repair of DSBs
JF  - Nucleic Acids Research
VL  - 48
IS  - 2
SP  - 694-708
EP  - 694-708
PB  - Oxford University Press
SN  - 03051048
KW  - Genome integrity
KW  - repair and replication
UR  - https://doi.org/10.1093/nar/gkz1052
L2  - https://doi.org/10.1093/nar/gkz1052
N2  - The proper repair of deleterious DNA lesions such as double strand breaks prevents genomic instability and carcinogenesis. In yeast, the Rad52 protein mediates DSB repair via homologous recombination. In mammalian cells, despite the presence of the RAD52 protein, the tumour suppressor protein BRCA2 acts as the predominant mediator during homologous recombination. For decades, it has been believed that the RAD52 protein played only a back-up role in the repair of DSBs performing an error-prone single strand annealing (SSA). Recent studies have identified several new functions of the RAD52 protein and have drawn attention to its important role in genome maintenance. Here, we show that RAD52 activities are enhanced by interacting with a small and highly acidic protein called DSS1. Binding of DSS1 to RAD52 changes the RAD52 oligomeric conformation, modulates its DNA binding properties, stimulates SSA activity and promotes strand invasion. Our work introduces for the first time RAD52 as another interacting partner of DSS1 and shows that both proteins are important players in the SSA and BIR pathways of DSB repair.
ER  -

ŠTEFANOVIE, Barbora, Sarah R. HENGEL, Jarmila MLČOUŠKOVÁ, Jana PROCHAZKOVA, Mário ŠPÍREK, Fedor NIKULENKOV, Daniel NĚMEČEK, Brandon G. KOCH, Fletcher E. BAIN, Liping YU, Maria SPIES and Lumír KREJČÍ. DSS1 interacts with and stimulates RAD52 to promote the repair of DSBs. \textit{Nucleic Acids Research}. Oxford: Oxford University Press, 2020, vol.~48, No~2, p.~694-708. ISSN~0305-1048. Available from: https://dx.doi.org/10.1093/nar/gkz1052.

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