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Regulatory and Enzymatic Functions of recA Protein in Recombination and Postreplication Repair

  • P. Howard-Flanders
  • E. Cassuto
  • S. C. West
Part of the NATO Advanced Study Institutes Series book series (NSSA, volume 40)

Abstract

Investigations into the genetics of recombination, repair and prophage induction in E. coli, have uncovered a remarkable regulatory system involving the lexA gene product as repressor and the recA gene product. This system normally produces lexA and recA proteins at low constitutive levels. The recA protein is a highly specific, single stranded DNA dependent protease capable of cleaving lexA protein and also phage lambda repressor. Postreplication gaps or other damage that produced single stranded regions in the bacterial DNA, may cause recA protein to bind to the DNA. The resulting increase in protease activity leads to the lexA protein being cleaved and thus turns on the transcription of the genes including recA that are under negative control by lexA.

RecA protein is an ATPase and requires ATP for most reactions. It does not appear to have any nuclease activity. It catalyses the annealing of single strands and homlogous duplex DNA to form D loops. It binds to duplex DNA in complex ways. If the duplex contains single stranded regions, recA protein binds cooperatively and loads the duplex molecules, covering the duplex as well as the single stranded regions. It prepares duplex DNA containing one or more single stranded gaps for hydrogen bonding to intact homologous duplex DNA and promotes the formation of hydrogen bonded joint molecules, but but does not cut the intact homolog in preparation for joining in recombination and postreplication repair.

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Copyright information

© Plenum Press, New York 1981

Authors and Affiliations

  • P. Howard-Flanders
    • 1
  • E. Cassuto
    • 1
  • S. C. West
    • 1
  1. 1.Dept. Molecular Biophysics & Dept. Therapeutic RadiologyYale UniversityNew HavenUSA

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