The processivity factor beta controls DNA polymerase IV traffic during spontaneous mutagenesis and translesion synthesis in vivo

EMBO Rep. 2002 Jan;3(1):45-9. doi: 10.1093/embo-reports/kvf007. Epub 2001 Dec 19.


The dinB-encoded DNA polymerase IV (Pol IV) belongs to the recently identified Y-family of DNA polymerases. Like other members of this family, Pol IV is involved in translesion synthesis and mutagenesis. Here, we show that the C-terminal five amino acids of Pol IV are essential in targeting it to the beta-clamp, the processivity factor of the replicative DNA polymerase (Pol III) of Escherichia coli. In vivo, the disruption of this interaction obliterates the function of Pol IV in both spontaneous and induced mutagenesis. These results point to the pivotal role of the processivity clamp during DNA polymerase trafficking in the vicinity of damaged-template DNA.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / metabolism*
  • Benzo(a)pyrene
  • Binding Sites
  • DNA Adducts
  • DNA Damage
  • DNA Polymerase III / metabolism
  • DNA Polymerase beta / metabolism*
  • DNA Repair*
  • DNA Replication / physiology*
  • DNA, Bacterial / biosynthesis
  • Escherichia coli / enzymology
  • Escherichia coli / genetics
  • Escherichia coli Proteins*
  • Guanine
  • Mutagenesis*
  • Two-Hybrid System Techniques


  • Bacterial Proteins
  • DNA Adducts
  • DNA, Bacterial
  • DinB protein, E coli
  • Escherichia coli Proteins
  • Benzo(a)pyrene
  • Guanine
  • beta subunit, DNA polymerase III
  • DNA Polymerase III
  • DNA Polymerase beta