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Ubiquitin-Binding Domains in Y-Family Polymerases Regulate Translesion Synthesis
journal contribution
posted on 2023-06-07, 22:58 authored by Marzena Bienko, Catherine M Green, Nicola Crosetto, Fabian Rudolf, Grzegorz Zapart, Barry Coull, Patricia Kannouche, Gerhard Wider, Matthias Peter, Alan LehmannAlan Lehmann, Kay Hofmann, Ivan DikicTranslesion synthesis (TLS) is the major pathway by which mammalian cells replicate across DNA lesions. Upon DNA damage, ubiquitination of proliferating cell nuclear antigen (PCNA) induces bypass of the lesion by directing the replication machinery into the TLS pathway. Yet, how this modification is recognized and interpreted in the cell remains unclear. Here we describe the identification of two ubiquitin (Ub)¿binding domains (UBM and UBZ), which are evolutionarily conserved in all Y-family TLS polymerases (pols). These domains are required for binding of pol¿ and pol¿ to ubiquitin, their accumulation in replication factories, and their interaction with monoubiquitinated PCNA. Moreover, the UBZ domain of pol¿ is essential to efficiently restore a normal response to ultraviolet irradiation in xeroderma pigmentosum variant (XP-V) fibroblasts. Our results indicate that Ub-binding domains of Y-family polymerases play crucial regulatory roles in TLS.
History
Publication status
- Published
Journal
ScienceISSN
0036-8075Publisher
American Association for the Advancement of SciencePublisher URL
External DOI
Issue
5575Volume
310Page range
1821-1824Pages
4.0Department affiliated with
- Sussex Centre for Genome Damage Stability Publications
Notes
Significant part done in my lab. I had major intellectual input into this work, as our collaborators were not DNA repair experts, so I made many suggestions for critical experiments and the paper was written jointly. It described novel ubiquitin-binding domains in all members of the Y-family of DNA polymerases.Full text available
- No
Peer reviewed?
- Yes
Legacy Posted Date
2012-02-06Usage metrics
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