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Esc2 promotes Mus81 complex-activity via its SUMO-like and DNA binding domains
M. Sebesta, M. Urulangodi, B. Stefanovie, B. Szakal, M. Pacesa, M. Lisby, D. Branzei, L. Krejci,
Jazyk angličtina Země Anglie, Velká Británie
Typ dokumentu časopisecké články
Free Medical Journals od 1996
PubMed Central od 1974
Europe PubMed Central od 1974
Open Access Digital Library od 1996-01-01 do 2030-12-31
Open Access Digital Library od 1974-01-01
Open Access Digital Library od 1996-01-01
Open Access Digital Library od 1996-01-01
Medline Complete (EBSCOhost) od 1996-01-01
Oxford Journals Open Access Collection od 1996-01-01
ROAD: Directory of Open Access Scholarly Resources od 1974
Odkazy
PubMed
27694623
DOI
10.1093/nar/gkw882
Knihovny.cz E-zdroje
- MeSH
- chromatidy chemie metabolismus MeSH
- DNA fungální genetika metabolismus MeSH
- DNA vazebné proteiny chemie genetika metabolismus MeSH
- endonukleasy chemie genetika metabolismus MeSH
- Escherichia coli genetika metabolismus MeSH
- jaderné proteiny chemie genetika metabolismus MeSH
- klonování DNA MeSH
- křížová struktura DNA chemie metabolismus MeSH
- malé modifikační proteiny související s ubikvitinem chemie genetika metabolismus MeSH
- nestabilita genomu MeSH
- poškození DNA MeSH
- proteinové domény MeSH
- regulace genové exprese u hub * MeSH
- rekombinantní proteiny chemie genetika metabolismus MeSH
- replikace DNA MeSH
- Saccharomyces cerevisiae - proteiny chemie genetika metabolismus MeSH
- Saccharomyces cerevisiae genetika metabolismus MeSH
- vazba proteinů MeSH
- Publikační typ
- časopisecké články MeSH
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.
Department of Biology University of Copenhagen DK 2200 Copenhagen Denmark
IFOM the FIRC Institute of Molecular Oncology Via Adamello 16 IT 20139 Milan Italy
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- $a 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.
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