Skip to main content
. Author manuscript; available in PMC: 2012 Sep 16.
Published in final edited form as: FEBS Lett. 2011 Jun 1;585(18):2780–2785. doi: 10.1016/j.febslet.2011.05.053

Figure 2.

Figure 2

A model for the role of ELG1 in PCNA deubiquitylation. Upon encountering DNA damage, the replication machinery becomes stalled. PCNA is then monoubiquitylated, and a TLS polymerase is recruited to the damage site to replace the replicative polymerase (Polδ/ε) and bypass the lesion. Once bypass has occurred, ELG1, which becomes concentrated at stalled forks with distinct foci structures in the nucleus, binds to PCNA and recruits the USP1/UAF1 complex. USP1 deubiquitylates PCNA, displacing the TLS polymerase and allowing Polδ/ε to resume normal replication.