G-quadruplex structures bind to EZ-Tn5 transposase

Biochimie. 2020 Oct:177:190-197. doi: 10.1016/j.biochi.2020.07.022. Epub 2020 Aug 14.

Abstract

Next generation DNA sequencing and analysis of amplicons spanning the pharmacogene CYP2D6 suggested that the Nextera transposase used for fragmenting and providing sequencing priming sites displayed a targeting bias. This manifested as dramatically lower sequencing coverage at sites in the amplicon that appeared likely to form G-quadruplex structures. Since secondary DNA structures such as G-quadruplexes are abundant in the human genome, and are known to interact with many other proteins, we further investigated these sites of low coverage. Our investigation revealed that G-quadruplex structures are formed in vitro within the CYP2D6 pharmacogene at these sites, and G-quadruplexes can interact with the hyperactive Tn5 transposase (EZ-Tn5) with high affinity. These findings indicate that secondary DNA structures such as G-quadruplexes may represent preferential transposon integration sites and provide additional evidence for the role of G-quadruplex structures in transposition or viral integration processes.

Keywords: DNA:Protein interaction; G-quadruplex; G4; Non-B DNA; Tn5 transposase.

MeSH terms

  • Circular Dichroism
  • Cytochrome P-450 CYP2D6 / chemistry
  • Cytochrome P-450 CYP2D6 / genetics
  • Cytochrome P-450 CYP2D6 / metabolism*
  • DNA / chemistry
  • DNA / metabolism
  • G-Quadruplexes*
  • GC Rich Sequence
  • Gene Amplification
  • High-Throughput Nucleotide Sequencing
  • Humans
  • Kinetics
  • Nucleotide Motifs
  • Sequence Alignment
  • Surface Plasmon Resonance
  • Transposases / genetics*
  • Transposases / metabolism*

Substances

  • Tn5 transposase
  • DNA
  • Cytochrome P-450 CYP2D6
  • Transposases