EME1 and MUS81 (MIM 606591) form an endonuclease complex that cleaves branched DNA structures, especially those arising during stalled DNA replication.EME1 and MUS81 (MIM 606591) form an endonuclease
- Known as:
- EME1 MUS81 (MIM 606591) form endonuclease aggregate cleaves branched Desoxyribonucleic acid structures, especially arising stalled Desoxyribonucleic acid replication.EME1 MUS81 (MIM 606591) form endonuclease
- Catalog number:
- 26-729
- Product Quantity:
- 0.05 mg
- Category:
- -
- Supplier:
- Prosci
- Gene target:
- EME1 and MUS81 (MIM 606591) form endonuclease complex that cleaves branched DNA structures especially those arising during stalled replication.EME1
Related genes to: EME1 and MUS81 (MIM 606591) form an endonuclease complex that cleaves branched DNA structures, especially those arising during stalled DNA replication.EME1 and MUS81 (MIM 606591) form an endonuclease
- Gene:
- EME1 NIH gene
- Name:
- essential meiotic structure-specific endonuclease 1
- Previous symbol:
- -
- Synonyms:
- FLJ31364, MMS4L, SLX2A
- Chromosome:
- 17q21.33
- Locus Type:
- gene with protein product
- Date approved:
- 2004-01-27
- Date modifiied:
- 2015-02-24
- Gene:
- LINC00862 NIH gene
- Name:
- long intergenic non-protein coding RNA 862
- Previous symbol:
- C1orf98, SMIM16
- Synonyms:
- -
- Chromosome:
- 1q32.1
- Locus Type:
- RNA, long non-coding
- Date approved:
- 2005-05-31
- Date modifiied:
- 2017-06-16
- Gene:
- MIMT1 NIH gene
- Name:
- MER1 repeat containing imprinted transcript 1
- Previous symbol:
- -
- Synonyms:
- MIM1, NCRNA00067, LINC00067
- Chromosome:
- 19q13.43
- Locus Type:
- RNA, long non-coding
- Date approved:
- 2007-06-13
- Date modifiied:
- 2018-05-16
- Gene:
- MTLN NIH gene
- Name:
- mitoregulin
- Previous symbol:
- NCRNA00116, LINC00116, SMIM37
- Synonyms:
- MOXI
- Chromosome:
- 2q13
- Locus Type:
- gene with protein product
- Date approved:
- 2008-09-12
- Date modifiied:
- 2018-07-17
- Gene:
- MTSS1 NIH gene
- Name:
- MTSS I-BAR domain containing 1
- Previous symbol:
- -
- Synonyms:
- KIAA0429, MIMA, MIMB, MIM
- Chromosome:
- 8q24.13
- Locus Type:
- gene with protein product
- Date approved:
- 2003-03-11
- Date modifiied:
- 2019-01-22
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- The synthetic lethal interaction between poly(ADP-ribose) polymerase (PARP) inhibition and homologous recombination (HR)-deficiency, particularly in BRCA1/2-mutant tumors, has emerged as an effective strategy for cancer therapy. GEN1, a structure-selective endonuclease that resolves Holliday junctions (HJs) during HR, represents an attractive antitumor target. However, effective small-molecule GEN1 inhibitors have yet to be reported. Here, we established a fluorescence resonance energy transfer (FRET)-based high-throughput screening platform and identified the natural flavonoid scutellarin (SCU) as a specific inhibitor of human GEN1. SCU selectively inhibited GEN1 endonuclease activity against both 5'-flap and HJ DNA substrates, with no effect on other tested structure-selective endonucleases, such as SLX1-SLX4 and MUS81-EME1. Mechanistic studies showed that SCU does not disrupt GEN1-DNA binding but instead binds to the catalytic center of GEN1, thereby inhibiting its endonuclease activity. In HCT116 cells, SCU acted in synergy with the PARP inhibitor olaparib to markedly impair DNA double-strand break (DSB) repair, increase γH2AX accumulation, induce G2/M cell cycle arrest, and suppress cell migration. Notably, the SCU/olaparib combination produced robust synthetic lethality in both HCT116 and HeLa cells, resulting in substantial inhibition of cell viability and colony formation. Our study identifies SCU as a novel selective GEN1 inhibitor, and suggests a new therapeutic strategy that combines GEN1 inhibitors with PARP inhibitors for cancer treatment. - Source: PubMed
Publication date: 2026/08/18
Zhan BinbinZhong YichenChen XueningDai YijunDu LiyangLin ZhonghuiLi Zuoan - SLX4 is a scaffold protein pivotal in genome protection mechanisms ranging from homologous recombination and interstrand cross-link (ICL) repair to mechanisms that deal with challenged DNA replication. Many of human SLX4 functions rely on its ability to interact and control the XPF-ERCC1, MUS81-EME1, and SLX1 structure-specific endonucleases. Interaction with MUS81 relies on the conserved SAP domain of SLX4. Since the same domain in yeast Slx4 orthologs does not interact with Mus81, we investigated whether human SLX4 SAP might have retained some ancestral MUS81-independent functions. We show that human SLX4 SAP binds DNA with a preference for branched structures such as Holliday junctions. We further discovered that phosphorylation of SLX4 SAP by CDK1, which promotes interaction with MUS81, inhibits DNA binding. We identified separation of function mutants that impair either DNA or MUS81 binding. Binding to MUS81 is required in response to ICL-inducing agents, methyl methanesulfonate (MMS), TOP1, and PARP inhibition. Instead, DNA binding is required in response to ICL-inducing agents and MMS but not after TOP1 or PARP inhibition. Our work indicates that phosphorylation by CDK1 acts as a regulatory switch between DNA binding and MUS81-dependent functions of SLX4, to accommodate specific DNA lesions or secondary structures. - Source: PubMed
Scaglione SarahGaillard Pierre-Henri - Recombinational repair provides an important pathway for the repair of DNA double strand breaks that arise in mitotic and meiotic cells. Homologous pairing and strand exchange leads to the formation of DNA intermediates that are linked by double Holliday junctions, and these need to be resolved prior to chromosome segregation and cell division. In mitotic cells, resolution occurs by either of two distinct pathways (i) Nucleolytic cleavage by GEN1 or SLX1-SLX4-MUS81-EME1-XPF-ERCC1 (SMX complex), or (ii) dissolution mediated by BLM-TopoIIIα-RMI1-RMI2 (BTRR complex). To facilitate the biochemical analysis of these pathways, we previously developed a novel methodology, involving DNAzyme self-cleavage, to generate 1.8-kb long DNA molecules containing dHJs. This involved the sequential annealing of precursor ssDNAs, which were first individually isolated through multiple rounds of gel purification and ethanol precipitation, but unfortunately the method was laborious and inefficient as considerable DNA losses were incurred at each step. Here, we describe a significantly improved methodology, that increases both the efficiency and yield without impacting the quality of the dHJs produced. The new method is rapid and simple, requiring only basic molecular biology expertise, and results in the formation of dHJs that make ideal substrates for the biochemical analysis of dissolution and resolution reaction in vitro. - Source: PubMed
Publication date: 2026/03/25
Shah Punatar RajveeHo Han NWest Stephen C - Faithful genome transmission depends on the timely removal of branched DNA intermediates. This task is executed by the SMX tri-nuclease, a mitosis-specific complex containing three structure-selective endonucleases (SLX1, MUS81-EME1, and XPF-ERCC1) bound to the SLX4 scaffold. A critical step in SMX assembly is the recruitment of MUS81-EME1 to SLX4 in early mitosis, a process tightly regulated by cell-cycle kinases. Mechanistically, CDK1-dependent phosphorylation of SLX4 promotes folding of its SAP domain, which strengthens the SLX4-MUS81 interaction. Here, we define a site-specific phosphorylation code that stabilizes complementary structures in the SLX4-MUS81 interface. Phosphorylation of SLX4 T1571 is required for partial SAP domain folding, pre-organizing the MUS81 binding surface and reducing the entropic penalty of folding upon binding. Co-phosphorylation at T1561 enhances structural stability and promotes intermolecular β-sheet formation with MUS81, providing enthalpic stabilization. Dual-site phosphorylation converts a relatively weak interaction into a high-affinity complex that stimulates MUS81-EME1 nuclease activity. In human cells, both phosphorylation sites are required for robust SMX assembly and genome stability maintenance. Collectively, our findings reveal the structural basis for how CDK1-cyclin B controls SMX assembly in mitosis. More broadly, the SLX4-MUS81 complex illustrates how phosphorylation fine-tunes marginally stable protein interfaces at the boundary of order and disorder. - Source: PubMed
Payliss Brandon JYun Hwa YoungDoshi SarinaLemak AlexanderTse Ying Wah EAprosoff Camila MHouliston ScottArrowsmith Cheryl HWyatt Haley D M - Helicases and endonucleases play crucial roles in genome maintenance by unwinding or cleaving various forms of DNA and RNA structures in order to facilitate essential biological processes, such as DNA replication and recombination. Here, we identified fission yeast Dbl2 as a potential interactor of several complexes that exhibit either helicase or endonuclease activity, namely Fml1-MHF, SCF, Rqh1-Top3-Rmi1, and Mus81-Eme1. In vitro, Dbl2 binds to DNA, with a preference for branched molecules, such as D-loops, mobile Holliday junctions, and fork structures, making it a good candidate to play a central role in modulating the activity of helicases and endonucleases during replication and recombination repair. Previously, we showed that Dbl2 recruits Fbh1 to the ongoing homologous recombination sites, affecting the Rad51-nucleofilament. In this study, we determined that deleting dbl2 in an fbh1Δ background did not increase sensitivity to DNA-damaging agents or the frequency of Tf2 ectopic recombination. Therefore, Dbl2 and Fbh1 might be involved in the same molecular pathway, maintaining genome integrity by hindering ectopic recombination at repetitive elements. - Source: PubMed
Publication date: 2025/07/01
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