Translesion synthesis by the UmuC family of DNA polymerases

Mutat Res. 2001 Jul 12;486(2):59-70. doi: 10.1016/s0921-8777(01)00089-1.

Abstract

Translesion synthesis is an important cellular mechanism to overcome replication blockage by DNA damage. To copy damaged DNA templates during replication, specialized DNA polymerases are required. Translesion synthesis can be error-free or error-prone. From E. coli to humans, error-prone translesion synthesis constitutes a major mechanism of DNA damage-induced mutagenesis. As a response to DNA damage during replication, translesion synthesis contributes to cell survival and induced mutagenesis. During 1999-2000, the UmuC superfamily had emerged, which consists of the following prototypic members: the E. coli UmuC, the E. coli DinB, the yeast Rad30, the human RAD30B, and the yeast Rev1. The corresponding biochemical activities are DNA polymerases V, IV, eta, iota, and dCMP transferase, respectively. Recent studies of the UmuC superfamily are summarized and evidence is presented suggesting that this family of DNA polymerases is involved in translesion DNA synthesis.

Publication types

  • Review

MeSH terms

  • Bacterial Proteins*
  • DNA Damage*
  • DNA Polymerase beta / metabolism
  • DNA Replication*
  • DNA-Directed DNA Polymerase / classification
  • DNA-Directed DNA Polymerase / metabolism*
  • Escherichia coli Proteins*
  • Fungal Proteins / metabolism
  • Models, Genetic
  • Nucleotidyltransferases / metabolism
  • Proteins / metabolism
  • Saccharomyces cerevisiae Proteins*

Substances

  • Bacterial Proteins
  • Escherichia coli Proteins
  • Fungal Proteins
  • Proteins
  • Saccharomyces cerevisiae Proteins
  • UmuC protein, E coli
  • DNA Polymerase beta
  • Nucleotidyltransferases
  • REV1 protein, S cerevisiae
  • DNA polymerase V, E coli
  • DNA-Directed DNA Polymerase
  • POLK protein, human
  • Rad30 protein