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Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-56817

Markkanen, E; van Loon, B; Ferrari, E; Hübscher, U (2011). Ubiquitylation of DNA polymerase λ. FEBS Letters, 585(18):2826-2830.

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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.


8 citations in Web of Science®
8 citations in Scopus®
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Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:05 Vetsuisse Faculty > Institute of Veterinary Biochemistry and Molecular Biology
Dewey Decimal Classification:570 Life sciences; biology
Deposited On:28 Feb 2012 13:16
Last Modified:04 Dec 2013 01:45
Publisher DOI:10.1016/j.febslet.2011.03.069
PubMed ID:21486570

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