ArticleNucleic acids research2013
Ubiquitin mediates the physical and functional interaction between human DNA polymerases η and ι.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 26 citations in OpenAlex.
- Overlapping RAD18-and DNA-binding interfaces in DNA polymerase η contribute to UV-induced DNA damage tolerance.The Journal of biological chemistry · 2026Article
- Human DNA polymerase η is regulated by mutually exclusive mono-ubiquitination and mono-NEDDylation.Nucleic acids research · 2026Article
- E3 ubiquitin ligase RNF2 protects polymerase ι from destabilization.Biochimica et biophysica acta. Molecular cell research · 2024Article
- A Novel Interaction Between RAD23A/B and Y-family DNA Polymerases.Journal of molecular biology · 2023Article
- DNA Polymerase ι Interacts with Both the TRAF-like and UBL1-2 Domains of USP7.Journal of molecular biology · 2021Article
- Review
- DNA polymerase ι is acetylated in response to SScientific reports · 2019Article
- Review
- Eukaryotic Translesion DNA Synthesis on the Leading and Lagging Strands: Unique Detours around the Same Obstacle.Chemical reviews · 2017Review
- Translesion DNA polymerases in eukaryotes: what makes them tick?Critical reviews in biochemistry and molecular biology · 2017Review
- Mouse DNA polymerase ι lacking the forty-two amino acids encoded by exon-2 is catalytically inactive in vitro.DNA repair · 2017Article
- DNA polymerase ι functions in the generation of tandem mutations during somatic hypermutation of antibody genes.The Journal of experimental medicine · 2016Article
- The Regulation of DNA Damage Tolerance by Ubiquitin and Ubiquitin-Like Modifiers.Frontiers in genetics · 2016Review
- Functions of Ubiquitin and SUMO in DNA Replication and Replication Stress.Frontiers in genetics · 2016Review
- Posttranslational Regulation of Human DNA Polymerase ι.The Journal of biological chemistry · 2015Article
- Different types of interaction between PCNA and PIP boxes contribute to distinct cellular functions of Y-family DNA polymerases.Nucleic acids research · 2015Article
- Regulation of translesion DNA synthesis: Posttranslational modification of lysine residues in key proteins.DNA repair · 2015Review
- DNA damage-specific deubiquitination regulates Rad18 functions to suppress mutagenesis.The Journal of cell biology · 2014Article
- The steric gate of DNA polymerase ι regulates ribonucleotide incorporation and deoxyribonucleotide fidelity.The Journal of biological chemistry · 2014Article
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
Human DNA polymerases η and ι are best characterized for their ability to facilitate translesion DNA synthesis (TLS). Both polymerases (pols) co-localize in 'replication factories' in vivo after cells are exposed to ultraviolet light and this co-localization is mediated through a physical interaction between the two TLS pols. We have mapped the polη-ι interacting region to their respective ubiquitin-binding domains (UBZ in polη and UBM1 and UBM2 in polι), and demonstrate that ubiquitination of either TLS polymerase is a prerequisite for their physical and functional interaction. Importantly, while monoubiquitination of polη precludes its ability to interact with proliferating cell nuclear antigen (PCNA), it enhances its interaction with polι. Furthermore, a polι-ubiquitin chimera interacts avidly with both polη and PCNA. Thus, the ubiquitination status of polη, or polι plays a key regulatory function in controlling the protein partners with which each polymerase interacts, and in doing so, determines the efficiency of targeting the respective polymerase to stalled replication forks where they facilitate TLS.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.