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Damaged replication forks tolerate USP7 to maintain genome stability.

Anastasia Zlatanou1, Grant S Stewart1

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The deubiquitylating enzyme USP7 protects RAD18 from degradation, ensuring faithful genome duplication through DNA damage tolerance (DTT). This discovery highlights USP7

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Area of Science:

  • Molecular biology
  • Genetics
  • Biochemistry

Background:

  • DNA damage tolerance (DTT) is crucial for maintaining genome stability during replication.
  • Protein ubiquitylation and deubiquitylation are key regulatory processes in DTT.
  • RAD18 is a known factor involved in promoting DTT.

Purpose of the Study:

  • To identify novel components of the DTT machinery.
  • To elucidate the regulatory mechanisms controlling RAD18 function.
  • To investigate the role of deubiquitylating enzymes in DTT.

Main Methods:

  • Proteasome activity assays
  • Ubiquitylation assays
  • Western blotting
  • Immunoprecipitation

Main Results:

  • USP7 was identified as a deubiquitylating enzyme involved in DTT.
  • USP7 protects RAD18 from proteasome-dependent degradation.
  • USP7 deubiquitylation activity is critical for RAD18 stability and DTT.

Conclusions:

  • USP7 is a novel component of the DTT pathway.
  • USP7 stabilizes RAD18 by preventing its proteasomal degradation.
  • Regulation of RAD18 stability by USP7 is essential for faithful genome duplication.