Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Arabidopsis thaliana Y-family DNA polymerase eta catalyses translesion synthesis and interacts functionally with PCNA2.

The Plant journal : for cell and molecular biology - 1 Sept 2008

Anderson Heather J, Vonarx Edward J, Pastushok Landon, Nakagawa Mayu, Katafuchi Atsushi, Gruz Petr, Di Rubbo Antonio, Grice Desma M, Osmond Megan J, Sakamoto Ayako N, Nohmi Takehiko, Xiao Wei, Kunz Bernard A

Abstract excerpt

SUMMARY: Upon blockage of chromosomal replication by DNA lesions, Y-family polymerases interact with monoubiquitylated proliferating cell nuclear antigen (PCNA) to catalyse translesion synthesis (TLS) and restore replication fork progression. Here, we assessed the roles of Arabidopsis thaliana POLH, which encodes a homologue of Y-family polymerase eta (Poleta), PCNA1 and PCNA2 in TLS-mediated UV resistance. A...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to DNA-Directed DNA Polymerase
Share to DNA Replication

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutagenesis, Insertional

Share to Plant Roots

Share to Proliferating Cell Nuclear Antigen

Share to RNA, Plant

Share to Two-Hybrid System Techniques

Share to Ultraviolet Rays

Source

Identifiers

PMID: 18494853
DOI: 10.1111/j.1365-313X.2008.03562.x

Genes

PCNA
POLH

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Arabidopsis thaliana Y-family DNA polymerase eta catalyses translesion synthesis and interacts functionally with PCNA2.PMID 18494853Read ↗

Ubiquitin-binding domains in Y-family polymerases regulate translesion synthesis.Semantic proximity Read ↗

DNA polymerase eta lacking the ubiquitin-binding domain promotes replicative lesion bypass in humans cells.Semantic proximity Read ↗

Roles of PCNA-binding and ubiquitin-binding domains in human DNA polymerase eta in translesion DNA synthesis.Semantic proximity Read ↗

Photo-activatable Ub-PCNA probes reveal new structural features of the Saccharomyces cerevisiae Polη/PCNA complex.Semantic proximity Read ↗

Requirement of DNA polymerase eta for error-free bypass of UV-induced CC and TC photoproducts.Semantic proximity Read ↗

Pirh2 E3 ubiquitin ligase monoubiquitinates DNA polymerase eta to suppress translesion DNA synthesis.Semantic proximity Read ↗

Mutations in the ubiquitin binding UBZ motif of DNA polymerase eta do not impair its function in translesion synthesis during replication.Semantic proximity Read ↗

Different types of interaction between PCNA and PIP boxes contribute to distinct cellular functions of Y-family DNA polymerases.Semantic proximity Read ↗

Similarities and differences between Arabidopsis PCNA1 and PCNA2 in complementing the yeast DNA damage tolerance defect.Semantic proximity Read ↗

Constitutive fusion of ubiquitin to PCNA provides DNA damage tolerance independent of translesion polymerase activities.Semantic proximity Read ↗

Physical and functional interactions of human DNA polymerase eta with PCNA.Semantic proximity Read ↗

DNA-damage tolerance mediated by PCNA*Ub fusions in human cells is dependent on Rev1 but not Polη.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.