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.
Other formats:   BibTeX LaTeX RIS
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
Original language English
Type of outcome Article in a journal
Field of Study 10608 Biochemistry and molecular biology
Country of publisher United Kingdom of Great Britain and Northern Ireland
Confidentiality degree is not subject to a state or trade secret
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
Tags EL OK, podil
Tags International impact, Reviewed
Changed by Changed by: Soňa Böhmová, učo 232884. Changed: 18/3/2018 16:35.
Abstract
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 projectName: Endonuleazová a translokázová aktivita v restričních-modifikáčních komplexéch typu I
Investor: Czech Science Foundation
GA13-26629S, research and development projectName: SUMO a stability genomu
Investor: Czech Science Foundation
MUNI/M/1894/2014, interní kód MUName: Development of new MUS81 nuclease inhibitors as chemical biology probe with clinical progression
Investor: Masaryk University, INTERDISCIPLINARY - Interdisciplinary research projects
PrintDisplayed: 24/4/2024 15:31