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Dbf4-dependent kinase finetunes Ino80 function at chromosome replication origins.

Priyanka Bansal1, Shibojyoti Lahiri1, Chandni Natalia Kumar1

  • 1Biomedical Center Munich (BMC), Division of Molecular Biology, Faculty of Medicine, Ludwig-Maximilians-Universität München, Munich, Martinsried, Germany.

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Summary
This summary is machine-generated.

The Dbf4-Dependent Kinase (DDK) regulates DNA replication by phosphorylating targets beyond the MCM complex. It stabilizes the INO80 chromatin remodeler, promoting replication and stress response.

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Area of Science:

  • Molecular Biology
  • Cell Cycle Regulation
  • Chromatin Dynamics

Background:

  • The Dbf4-Dependent Kinase (DDK) is crucial for S phase progression.
  • DDK phosphorylates the minichromosome maintenance (MCM) complex to initiate DNA replication.
  • Limited knowledge exists regarding other DDK substrates and functions.

Purpose of the Study:

  • To identify novel nuclear DDK targets and understand their roles.
  • To investigate the impact of DDK phosphorylation on chromatin remodeling complexes.

Main Methods:

  • Utilized a two-pronged mass spectrometry approach.
  • Analyzed the nuclear phosphoproteome to identify DDK-dependent phosphorylation sites.

Main Results:

  • Identified approximately 400 DDK-dependent phosphorylation targets.
  • Discovered Arp8, a subunit of the INO80 chromatin remodeling complex, as a novel DDK target.
  • Arp8 phosphorylation stabilizes the INO80 complex and optimizes nucleosome spacing at replication origins.

Conclusions:

  • DDK regulates chromatin remodeling complexes, specifically the INO80 complex via Arp8 phosphorylation.
  • This regulation fine-tunes chromatin architecture to facilitate DNA replication and enhance the replication stress response.
  • DDK controls both core replication machinery and factors establishing replication-permissive chromatin states.