Human PSF concentrates DNA and stimulates duplex capture in DMC1-mediated homologous pairing

Nucleic Acids Res. 2012 Apr;40(7):3031-41. doi: 10.1093/nar/gkr1229. Epub 2011 Dec 9.

Abstract

PSF is considered to have multiple functions in RNA processing, transcription and DNA repair by mitotic recombination. In the present study, we found that PSF is produced in spermatogonia, spermatocytes and spermatids, suggesting that PSF may also function in meiotic recombination. We tested the effect of PSF on homologous pairing by the meiosis-specific recombinase DMC1, and found that human PSF robustly stimulated it. PSF synergistically enhanced the formation of a synaptic complex containing DMC1, ssDNA and dsDNA during homologous pairing. The PSF-mediated DMC1 stimulation may be promoted by its DNA aggregation activity, which increases the local concentrations of ssDNA and dsDNA for homologous pairing by DMC1. These results suggested that PSF may function as an activator for the meiosis-specific recombinase DMC1 in higher eukaryotes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Cycle Proteins / metabolism*
  • DNA / metabolism*
  • DNA, Single-Stranded / metabolism
  • DNA-Binding Proteins / metabolism*
  • Homologous Recombination*
  • Humans
  • Male
  • Mice
  • Nuclear Proteins / metabolism
  • PTB-Associated Splicing Factor
  • Phosphate-Binding Proteins
  • RNA-Binding Proteins / biosynthesis
  • RNA-Binding Proteins / metabolism*
  • Rad51 Recombinase / metabolism
  • Spermatozoa / metabolism

Substances

  • Cell Cycle Proteins
  • DNA, Single-Stranded
  • DNA-Binding Proteins
  • Dmc1 protein, mouse
  • Nuclear Proteins
  • PTB-Associated Splicing Factor
  • Phosphate-Binding Proteins
  • RNA-Binding Proteins
  • DNA
  • Rad51 Recombinase
  • Rad51 protein, mouse
  • DMC1 protein, human