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1 Q&As
Facts about Crossover junction endonuclease EME1.
May be required in mitosis for the processing of stalled or collapsed replication forks. .
Human | |
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Gene Name: | EME1 |
Uniprot: | Q96AY2 |
Entrez: | 146956 |
Belongs to: |
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EME1/MMS4 family |
crossover junction endonuclease EME1; EC 3.1.22; EC 3.1.22.-; essential meiotic endonuclease 1 homolog 1 (S. pombe); essential meiotic endonuclease 1 homolog 2; FLJ31364; hMMS4; homolog of yeast EME1 endonuclease; MMS4 homolog; MMS4; MMS4L; SLX2 structure-specific endonuclease subunit homolog A; SLX2A
Mass (kDA):
63.252 kDA
Human | |
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Location: | 17q21.33 |
Sequence: | 17; NC_000017.11 (50373220..50381483) |
Nucleus, nucleolus. Recruited to regions of DNA damage in S-phase cells.
In this article, we will look at the history of the EME1 Marker and explore some of the best uses for it. This article will also go over the Boster Bio: Best Uses For The EME1 Marker and its uses in biological assays. To start with, the EME1 Marker has been present in many animal samples. Boster Bio, for instance, uses rabbit and mouse to develop its antibodies.
The EME1 Marker is one of many biomarkers used in biological assays. Several biological assays use antibodies to detect EGFEM1P. These antibodies are either monoclonal or polyclonal, and they react with EGFEM1P in various animal samples. Boster Bio uses rabbit and mouse as the model animals for developing its EME1 antibodies.
The EME1 gene encodes an endonuclease that mediates the clearance of Holliday junctions. This protein is involved in several biological processes, including cell proliferation, DNA damage response, and apoptosis. It has also been shown to regulate enzymatic activity and intracellular localization. However, further research is necessary to determine its optimal use. Here, we discuss the best uses of EME1 in various research applications.
Recent research has suggested that the EME1 marker may be associated with breast cancer risk. A case-control study at a hospital looked at two variants of the gene, Ile350Thr: rs12450550T and Glu69Asp: rs3760413T>G. Researchers compared the EME1 variants in 748 women with breast cancer and a matched group of 778 cancer-free women.
Molecular and biochemical data suggest that the primary function of Mus81-Eme1 is similar to that of the enzyme in yeast. The enzyme is involved in cleaving HJs by targeting aberrant replication fork intermediates. Defects in the nuclease activity in mammalian cells are thought to contribute to genomic instability and carcinogenesis. However, further research is needed to clarify the role of this gene in human disease.
In humans, the EME1 gene encodes a protein with a molecular mass of 65 kDa. Another version of the EME1 gene, the EME1 protein, has been identified in a neuroblastoma cell line. The EME2 gene is located on 16p13.3 and encodes a 245 amino acid protein with a molecular mass of 26 kD.
Researchers have proposed two mechanisms for Eme1 up-regulation. One mechanism involves protein stabilization and mRNA synthesis. The other mechanism is an alternative pathway that may up-regulate Eme1 expression. However, this method requires a larger study sample. As a result, EME1 expression levels are not directly related to tumor size. They also appear to be important for the maintenance of genomic integrity. A gene that affects EME1 is associated with increased risk of cancer.
The cisplatin sensitivity prediction by assessing Eme1 expression in a human tumor cell line has the potential to improve cancer therapy. In addition, Eme1 is associated with a higher percentage of cells escaping the spindle checkpoint, a process that induces cell death. In the case of HCT116 cells, Eme1 haploinsufficiency resulted in hypersensitivity to cisplatin, a common therapy for advanced cancers.
The cis-EGFR-Src inhibitor inhibits STAT3 binding to DNA. This resulted in accumulation of cells in the G2 phase. Thus, the interactions between cis-EGFR and Eme1 are also important in vivo cell cultures. In a previous study, IL-6 induced the co-precipitation of the two proteins in E. coli. The two proteins have been found to be regulated by STAT3, and this activity confirms the specificity of their interaction.
PMID: 12686547 by Oegruenc M., et al. Identification and characterization of human MUS81-MMS4 structure- specific endonuclease.
PMID: 12721304 by Ciccia A., et al. Identification and characterization of the human mus81-eme1 endonuclease.