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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,
Language English Country England, Great Britain
Document type Journal Article
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PubMed
27694623
DOI
10.1093/nar/gkw882
Knihovny.cz E-resources
- MeSH
- Chromatids chemistry metabolism MeSH
- DNA, Fungal genetics metabolism MeSH
- DNA-Binding Proteins chemistry genetics metabolism MeSH
- Endonucleases chemistry genetics metabolism MeSH
- Escherichia coli genetics metabolism MeSH
- Nuclear Proteins chemistry genetics metabolism MeSH
- Cloning, Molecular MeSH
- DNA, Cruciform chemistry metabolism MeSH
- Small Ubiquitin-Related Modifier Proteins chemistry genetics metabolism MeSH
- Genomic Instability MeSH
- DNA Damage MeSH
- Protein Domains MeSH
- Gene Expression Regulation, Fungal * MeSH
- Recombinant Proteins chemistry genetics metabolism MeSH
- DNA Replication MeSH
- Saccharomyces cerevisiae Proteins chemistry genetics metabolism MeSH
- Saccharomyces cerevisiae genetics metabolism MeSH
- Protein Binding MeSH
- Publication type
- Journal Article 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
References provided by Crossref.org
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