Abstract:
: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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Markkanen E,van Loon B,Ferrari E,Hübscher Udoi
10.1016/j.febslet.2011.03.069subject
Has Abstractpub_date
2011-09-16 00:00:00pages
2826-30issue
18eissn
0014-5793issn
1873-3468pii
S0014-5793(11)00249-3journal_volume
585pub_type
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