Ubiquitylation of DNA polymerase λ

FEBS Lett. 2011 Sep 16;585(18):2826-30. doi: 10.1016/j.febslet.2011.03.069. Epub 2011 Apr 8.


DNA polymerase (pol) λ, one of the 15 cellular pols, belongs to the X family. It is a small 575 amino-acid protein containing a polymerase, a dRP-lyase, a proline/serine rich and a BRCT domain. Pol λ shows various enzymatic activities including DNA polymerization, terminal transferase and dRP-lyase. It has been implicated to play a role in several DNA repair pathways, particularly base excision repair (BER), non-homologous end-joining (NHEJ) and translesion DNA synthesis (TLS). Similarly to other DNA repair enzymes, pol λ undergoes posttranslational modifications during the cell cycle that regulate its stability and possibly its subcellular localization. Here we describe our knowledge about ubiquitylation of pol λ and the impact of this modification on its regulation.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Binding Sites / genetics
  • DNA / genetics
  • DNA / metabolism
  • DNA Damage
  • DNA Ligase ATP
  • DNA Ligases / metabolism
  • DNA Polymerase beta / genetics
  • DNA Polymerase beta / metabolism*
  • DNA Repair*
  • DNA Replication*
  • DNA-Binding Proteins / metabolism
  • Humans
  • Ubiquitination*


  • DNA-Binding Proteins
  • XRCC4 protein, human
  • DNA
  • DNA polymerase beta2
  • DNA Polymerase beta
  • DNA Ligases
  • DNA Ligase ATP