The Bacillus subtilis addAB genes are fully functional in Escherichia coli

Mol Microbiol. 1993 Mar;7(6):915-23. doi: 10.1111/j.1365-2958.1993.tb01182.x.


An Escherichia coli recBCD deletion mutant was transformed with plasmids containing the Bacillus subtilis add genes. The transformants had relatively high ATP-dependent exonuclease- and ATP-dependent helicase activities, and their viability, the ability to repair u.v.-damaged DNA and the recombination in conjugation were nearly completely restored. The B. subtilis Add enzyme did not show Chi-activity in phage lambda recombination. The individual B. subtilis Add proteins were not able to form an enzymatically active complex with the E. coli RecB,C,D proteins, and they could not complement the recB,C,D deficiency. Evidence is presented that only two subunits are involved in the B. subtilis ATP-dependent exonuclease. This is in contrast to E. coli in which the RecBCD enzyme consists of three subunits.

Publication types

  • Comparative Study

MeSH terms

  • Bacillus subtilis / genetics*
  • Bacillus subtilis / metabolism
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Bacteriophages / genetics
  • DNA Helicases / genetics
  • DNA Helicases / metabolism
  • DNA Repair
  • DNA, Viral / genetics
  • Escherichia coli / metabolism*
  • Escherichia coli Proteins*
  • Exodeoxyribonuclease V
  • Exodeoxyribonucleases / genetics
  • Exodeoxyribonucleases / metabolism
  • Genetic Complementation Test
  • Genetic Vectors
  • Plasmids
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism*
  • Recombination, Genetic
  • Species Specificity
  • Transformation, Bacterial


  • Bacterial Proteins
  • DNA, Viral
  • Escherichia coli Proteins
  • Recombinant Fusion Proteins
  • Exodeoxyribonucleases
  • AddA protein, Bacillus subtilis
  • AddB protein, Bacillus subtilis
  • Exodeoxyribonuclease V
  • exodeoxyribonuclease V, E coli
  • DNA Helicases