Metalloprotease SPRTN/DVC1 Orchestrates Replication-Coupled DNA-Protein Crosslink Repair

Mol Cell. 2016 Nov 17;64(4):704-719. doi: 10.1016/j.molcel.2016.09.032. Epub 2016 Oct 27.

Abstract

The cytotoxicity of DNA-protein crosslinks (DPCs) is largely ascribed to their ability to block the progression of DNA replication. DPCs frequently occur in cells, either as a consequence of metabolism or exogenous agents, but the mechanism of DPC repair is not completely understood. Here, we characterize SPRTN as a specialized DNA-dependent and DNA replication-coupled metalloprotease for DPC repair. SPRTN cleaves various DNA binding substrates during S-phase progression and thus protects proliferative cells from DPC toxicity. Ruijs-Aalfs syndrome (RJALS) patient cells with monogenic and biallelic mutations in SPRTN are hypersensitive to DPC-inducing agents due to a defect in DNA replication fork progression and the inability to eliminate DPCs. We propose that SPRTN protease represents a specialized DNA replication-coupled DPC repair pathway essential for DNA replication progression and genome stability. Defective SPRTN-dependent clearance of DPCs is the molecular mechanism underlying RJALS, and DPCs are contributing to accelerated aging and cancer.

Keywords: DNA replication; DNA-dependent metalloprotease; DNA-protein crosslink repair; Ruijs-Aalfs/SPARTAN syndrome; SPARTAN/DVC1; aging; cancer.

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Cross-Linking Reagents / chemistry
  • DNA / chemistry*
  • DNA / genetics
  • DNA / metabolism
  • DNA Damage
  • DNA Repair*
  • DNA Replication*
  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / metabolism*
  • Etoposide / chemistry
  • Formaldehyde / chemistry
  • Gene Expression
  • Genomic Instability*
  • Humans
  • Kinetics
  • Mutation
  • Protein Binding
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Substrate Specificity
  • Syndrome
  • Ultraviolet Rays

Substances

  • Cross-Linking Reagents
  • DNA-Binding Proteins
  • SPRTN protein, human
  • Formaldehyde
  • Etoposide
  • DNA