Bacterial transformation: ComFA is a DNA-dependent ATPase that forms complexes with ComFC and DprA

Mol Microbiol. 2017 Sep;105(5):741-754. doi: 10.1111/mmi.13732. Epub 2017 Jul 28.

Abstract

Pneumococcal natural transformation contributes to genomic plasticity, antibiotic resistance development and vaccine escape. Streptococcus pneumoniae, like many other naturally transformable species, has evolved sophisticated protein machinery for the binding and uptake of DNA. Two proteins encoded by the comF operon, ComFA and ComFC, are involved in transformation but their exact molecular roles remain unknown. In this study, we provide experimental evidence that ComFA binds to single stranded DNA (ssDNA) and has ssDNA-dependent ATPase activity. We show that both ComFA and ComFC are essential for the transformation process in pneumococci. Moreover, we show that these proteins interact with each other and with other proteins involved in homologous recombination, such as DprA, thus placing the ComFA-ComFC duo at the interface between DNA uptake and DNA recombination during transformation.

MeSH terms

  • Adenosine Triphosphatases / genetics
  • Adenosine Triphosphatases / metabolism*
  • Bacterial Proteins / metabolism
  • DNA / metabolism
  • DNA, Single-Stranded / metabolism
  • DNA-Binding Proteins / metabolism*
  • Homologous Recombination
  • Membrane Proteins / metabolism
  • Protein Binding
  • Rec A Recombinases / metabolism
  • Recombination, Genetic
  • Streptococcus pneumoniae / genetics
  • Streptococcus pneumoniae / metabolism
  • Transformation, Bacterial / genetics
  • Transformation, Bacterial / physiology*

Substances

  • Bacterial Proteins
  • DNA, Single-Stranded
  • DNA-Binding Proteins
  • DprA protein, bacteria
  • Membrane Proteins
  • DNA
  • Rec A Recombinases
  • Adenosine Triphosphatases
  • single stranded DNA dependent ATPase