Esc2 promotes Mus81 complex-activity via its SUMO-like and DNA
binding domains

J 2017

Esc2 promotes Mus81 complex-activity via its SUMO-like and DNA binding domains

ŠEBESTA, Marek, Madhusoodanan URULANGODI, Barbora ŠTEFANOVIE, Barnabas SZAKAL, Martin PAČESA et. al.

Basic information

Original name

Esc2 promotes Mus81 complex-activity via its SUMO-like and DNA binding domains

Authors

ŠEBESTA, Marek (703 Slovakia, belonging to the institution), Madhusoodanan URULANGODI (380 Italy), Barbora ŠTEFANOVIE (703 Slovakia, belonging to the institution), Barnabas SZAKAL (380 Italy), Martin PAČESA (703 Slovakia, belonging to the institution), Michael LISBY (208 Denmark), Dana BRANZEI (380 Italy) and Lumír KREJČÍ (203 Czech Republic, guarantor, belonging to the institution)

Edition

Nucleic Acids Research, Oxford, Oxford University Press, 2017, 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

Impact factor

Impact factor: 11.561

RIV identification code

RIV/00216224:14110/17:00094560

Organization unit

Faculty of Medicine

DOI

http://dx.doi.org/10.1093/nar/gkw882

UT WoS

000396575100023

Keywords in English

SACCHAROMYCES-CEREVISIAE MUS81-MMS4; STRUCTURE-SPECIFIC ENDONUCLEASE; STIMULATES FLAP ENDONUCLEASE-1; UBIQUITIN-LIKE MODIFIER; HOMOLOGOUS RECOMBINATION; REPLICATION FORKS; STALLED REPLICATION; BUDDING YEAST; HOLLIDAY JUNCTIONS; GENOME INTEGRITY

Abstract

V originále

Replication across damaged DNA templates is accompanied by transient formation of sister chromatid junctions (SCJs). Cells lacking Esc2, an adaptor protein containing no known enzymatic domains, are defective in the metabolism of these SCJs. However, how Esc2 is involved in the metabolism of SCJs remains elusive. Here we show interaction between Esc2 and a structure-specific endonuclease Mus81- Mms4 (the Mus81 complex), their involvement in the metabolism of SCJs, and the effects Esc2 has on the enzymatic activity of the Mus81 complex. We found that Esc2 specifically interacts with the Mus81 complex via its SUMO-like domains, stimulates enzymatic activity of the Mus81 complex in vitro, and is involved in the Mus81 complex-dependent resolution of SCJs in vivo. Collectively, our data point to the possibility that the involvement of Esc2 in the metabolism of SCJs is, in part, via modulation of the activity of the Mus81 complex.

Links

GAP207/12/2323, research and development project

Name: Endonuleazová a translokázová aktivita v restričních-modifikáčních komplexéch typu I

Investor: Czech Science Foundation

GA13-26629S, research and development project

Name: SUMO a stability genomu

Investor: Czech Science Foundation

MUNI/M/1894/2014, interní kód MU

Name: Development of new MUS81 nuclease inhibitors as chemical biology probe with clinical progression

Investor: Masaryk University, INTERDISCIPLINARY - Interdisciplinary research projects

Citovat

ŠEBESTA, Marek, Madhusoodanan URULANGODI, Barbora ŠTEFANOVIE, Barnabas SZAKAL, Martin PAČESA, Michael LISBY, Dana BRANZEI and Lumír KREJČÍ. Esc2 promotes Mus81 complex-activity via its SUMO-like and DNA binding domains. Nucleic Acids Research. Oxford: Oxford University Press, 2017, vol. 45, No 1, p. 215-230. ISSN 0305-1048. Available from: https://dx.doi.org/10.1093/nar/gkw882.

@article{1357244,
   author = {Šebesta, Marek and Urulangodi, Madhusoodanan and Štefanovie, Barbora and Szakal, Barnabas and Pačesa, Martin and Lisby, Michael and Branzei, Dana and Krejčí, Lumír},
   article_location = {Oxford},
   article_number = {1},
   doi = {http://dx.doi.org/10.1093/nar/gkw882},
   keywords = {SACCHAROMYCES-CEREVISIAE MUS81-MMS4; STRUCTURE-SPECIFIC ENDONUCLEASE; STIMULATES FLAP ENDONUCLEASE-1; UBIQUITIN-LIKE MODIFIER; HOMOLOGOUS RECOMBINATION; REPLICATION FORKS; STALLED REPLICATION; BUDDING YEAST; HOLLIDAY JUNCTIONS; GENOME INTEGRITY},
   language = {eng},
   issn = {0305-1048},
   journal = {Nucleic Acids Research},
   title = {Esc2 promotes Mus81 complex-activity via its SUMO-like and DNA binding domains},
   volume = {45},
   year = {2017}
}

TY  - JOUR
ID  - 1357244
AU  - Šebesta, Marek - Urulangodi, Madhusoodanan - Štefanovie, Barbora - Szakal, Barnabas - Pačesa, Martin - Lisby, Michael - Branzei, Dana - Krejčí, Lumír
PY  - 2017
TI  - Esc2 promotes Mus81 complex-activity via its SUMO-like and DNA binding domains
JF  - Nucleic Acids Research
VL  - 45
IS  - 1
SP  - 215-230
EP  - 215-230
PB  - Oxford University Press
SN  - 03051048
KW  - SACCHAROMYCES-CEREVISIAE MUS81-MMS4
KW  - STRUCTURE-SPECIFIC ENDONUCLEASE
KW  - STIMULATES FLAP ENDONUCLEASE-1
KW  - UBIQUITIN-LIKE MODIFIER
KW  - HOMOLOGOUS RECOMBINATION
KW  - REPLICATION FORKS
KW  - STALLED REPLICATION
KW  - BUDDING YEAST
KW  - HOLLIDAY JUNCTIONS
KW  - GENOME INTEGRITY
N2  - Replication across damaged DNA templates is accompanied by transient formation of sister chromatid junctions (SCJs). Cells lacking Esc2, an adaptor protein containing no known enzymatic domains, are defective in the metabolism of these SCJs. However, how Esc2 is involved in the metabolism of SCJs remains elusive. Here we show interaction between Esc2 and a structure-specific endonuclease Mus81- Mms4 (the Mus81 complex), their involvement in the metabolism of SCJs, and the effects Esc2 has on the enzymatic activity of the Mus81 complex. We found that Esc2 specifically interacts with the Mus81 complex via its SUMO-like domains, stimulates enzymatic activity of the Mus81 complex in vitro, and is involved in the Mus81 complex-dependent resolution of SCJs in vivo. Collectively, our data point to the possibility that the involvement of Esc2 in the metabolism of SCJs is, in part, via modulation of the activity of the Mus81 complex.
ER  -

ŠEBESTA, Marek, Madhusoodanan URULANGODI, Barbora ŠTEFANOVIE, Barnabas SZAKAL, Martin PAČESA, Michael LISBY, Dana BRANZEI and Lumír KREJČÍ. Esc2 promotes Mus81 complex-activity via its SUMO-like and DNA binding domains. \textit{Nucleic Acids Research}. Oxford: Oxford University Press, 2017, vol.~45, No~1, p.~215-230. ISSN~0305-1048. Available from: https://dx.doi.org/10.1093/nar/gkw882.

Detailed Information on Publication Record