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indicate that SLX1 and MUS81 (show MUS81 Antibodies)-EME1 nucleases act together to resolve Holliday junctions (HJs) in a manner that requires tethering to SLX4 (show BTBD12 Antibodies).
Mus81 (show MUS81 Antibodies)-Eme1- and Rad54 (show RAD54L Antibodies)-mediated homologous recombination are involved in the same DNA replication-dependent interstrand crosslinks repair pathway
These findings link Eme1 with the replication-associated chromatin modifier functions of Np95 (show UHRF1 Antibodies) in the cellular response to DNA damage.
While Mus81 (show MUS81 Antibodies)-Eme1 shares several common features with members of the 5' flap (show ALOX5AP Antibodies) nuclease (show DCLRE1C Antibodies) family, the combined structural, biochemical, and biophysical analyses explain why Mus81 (show MUS81 Antibodies)-Eme1 preferentially cleaves 3' flap (show ALOX5AP Antibodies) DNA substrates with 5' nicked ends.
Data show that three structure-selective endonucleases, SLX1-SLX4 (show BTBD12 Antibodies), MUS81 (show MUS81 Antibodies)-EME1, and GEN1 (show GEN1 Antibodies), define two pathways of Holliday junctions (HJs) resolution in HeLa cells.
Data show that Mus81 (show MUS81 Antibodies)/Eme1-dependent DNA damage--rather than a global increase in replication-fork stalling--is the cause of incomplete replication in Chk1 (show CHEK1 Antibodies)-deficient cells.
Results demonstrate a novel role of Wee1 (show WEE1 Antibodies) in controlling Mus81 (show MUS81 Antibodies)-Eme1 and DNA replication in human cells.
EME-1 deficiency affects cell cycle progression and promotes DNA rereplication.
Mus81 (show MUS81 Antibodies)-Eme1 can ensure coordinate, bilateral cleavage of Holliday junction-like structures.
the crystal structure of the Mus81 (show MUS81 Antibodies)-Eme1 complex
results demonstrate a link between branch migration activity of hRad54 (show RAD54L Antibodies) and structure-specific endonuclease activity of hMus81-Eme1, suggesting that the Rad54 (show ATRX Antibodies) and Mus81 (show MUS81 Antibodies)-Eme1 proteins may cooperate in the processing of Holliday junction-like intermediates
Low Eme1 levels were more sensitive to the drug than tumors with high levels.
This gene encodes a protein that complexes with methyl methanesulfonate-sensitive UV-sensitive 81 protein to form an endonuclease complex. The encoded protein interacts with specifc DNA structures including nicked Holliday junctions, 3'-flap structures and aberrant replication fork structures. This protein may be involved in repairing DNA damage and in maintaining genomic stability. Alternative splicing results in multiple transcript variants.
essential meiotic endonuclease 1 homolog 1 (S. pombe)
, essential meiotic endonuclease 1 homolog 2
, probable crossover junction endonuclease EME2
, crossover junction endonuclease EME1
, MMS4 homolog
, SLX2 structure-specific endonuclease subunit homolog A
, essential meiotic endonuclease 1 homolog 1
, homolog of yeast EME1 endonuclease