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Engineering Artificial Factors to Specifically Manipulate Alternative Splicing in Human Cells
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Published on: April 26, 2017

Human MUS81 complexes stimulate flap endonuclease 1.

Yong-Keol Shin1, Tamir Amangyeld, Tuan A Nguyen

  • 1Department of Biological Sciences, Center for DNA Replication and Genome Instability, Korea Advanced Institute of Science and Technology, Daejeon, Korea.

The FEBS Journal
|May 4, 2012
PubMed
Summary
This summary is machine-generated.

Human FEN1 and MUS81-EME1/2 collaborate in DNA repair, with MUS81 enhancing FEN1

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Area of Science:

  • Molecular Biology
  • DNA Repair Mechanisms
  • Enzymology

Background:

  • The yeast Mus81-Mms4 complex is crucial for replication fork restart and removing toxic recombination intermediates.
  • Yeast FEN1 (Rad27) and Mus81-Mms4 exhibit mutual stimulation of nuclease activity.
  • Human homologs MUS81-EME1/2 and FEN1 are involved in DNA processing.

Purpose of the Study:

  • To investigate the interactions between human FEN1 and MUS81-EME1/2.
  • To compare the functional relationship between human homologs and their yeast counterparts.
  • To elucidate the mechanism of FEN1 stimulation by MUS81.

Main Methods:

  • In vitro nuclease activity assays.
  • Analysis of protein-protein interactions.
  • Michaelis-Menten kinetic analysis.
  • Immunofluorescence microscopy in human cells.

Main Results:

  • Human MUS81-EME1 and MUS81-EME2 enhance FEN1 activity, but not vice versa.
  • The MUS81 subunit alone, particularly its N-terminal half, binds and stimulates FEN1.
  • MUS81 increases FEN1 substrate interaction and turnover.
  • FEN1 and MUS81 co-localize in human cells after DNA damage.

Conclusions:

  • Human FEN1 and MUS81-EME1/2 exhibit functional cooperation in DNA processing, distinct from yeast mutual stimulation.
  • The MUS81 subunit is responsible for stimulating FEN1 activity.
  • This collaboration is vital for processing flap structures during DNA transactions like Okazaki fragment processing.