Journal article
Ubiquitylation of DNA polymerase λ.
- Markkanen E Institute for Veterinary Biochemistry and Molecular Biology, University of Zürich-Irchel, Winterthurerstrasse 190, 8057 Zürich, Switzerland.
- van Loon B
- Ferrari E
- Hübscher U
- 2011-04-14
Published in:
- FEBS letters. - 2011
Binding Sites
DNA
DNA Damage
DNA Ligase ATP
DNA Ligases
DNA Polymerase beta
DNA Repair
DNA Replication
DNA-Binding Proteins
Humans
Ubiquitination
English
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.
- Language
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- English
- Open access status
- hybrid
- Identifiers
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- DOI 10.1016/j.febslet.2011.03.069
- PMID 21486570
- Persistent URL
- https://sonar.ch/global/documents/165763
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