ArticleProceedings of the National Academy of Sciences of the United States of America2011
Crystal structures of two active proliferating cell nuclear antigens (PCNAs) encoded by Thermococcus kodakaraensis.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 32 citations in OpenAlex.
- Ribonucleotide errors, RNase HII, and ribonucleotide excision repair.Critical reviews in biochemistry and molecular biology · 2026Review
- DNA polymerase D temporarily connects primase to the CMG-like helicase before interacting with proliferating cell nuclear antigen.Nucleic acids research · 2021Article
- Two conformations of DNA polymerase D-PCNA-DNA, an archaeal replisome complex, revealed by cryo-electron microscopy.BMC biology · 2020Article
- Biochemical reconstitution and genetic characterization of the major oxidative damage base excision DNA repair pathway in Thermococcus kodakarensis.DNA repair · 2020Article
- An overview of 25 years of research on Thermococcus kodakarensis, a genetically versatile model organism for archaeal research.Folia microbiologica · 2020Review
- A global map of the protein shape universe.PLoS computational biology · 2019Article
- Defining the RNaseH2 enzyme-initiated ribonucleotide excision repair pathway in Archaea.The Journal of biological chemistry · 2017Article
- Cloning, recombinant production and crystallographic structure of Proliferating Cell Nuclear Antigen from radioresistant archaeonBiochemistry and biophysics reports · 2016Review
- PCNA-binding proteins in the archaea: novel functionality beyond the conserved core.Current genetics · 2016Review
- A small protein inhibits proliferating cell nuclear antigen by breaking the DNA clamp.Nucleic acids research · 2016Article
- Characterization of family D DNA polymerase from Thermococcus sp. 9°N.Extremophiles : life under extreme conditions · 2014Article
- A novel mechanism for regulating the activity of proliferating cell nuclear antigen by a small protein.Nucleic acids research · 2014Article
- Post-translational modifications of proliferating cell nuclear antigen: A key signal integrator for DNA damage response (Review).Oncology letters · 2014Article
- Conformational analysis of processivity clamps in solution demonstrates that tertiary structure does not correlate with protein dynamics.Structure (London, England : 1993) · 2014Article
- Diversity of the DNA replication system in the Archaea domain.Archaea (Vancouver, B.C.) · 2014Review
- Thermococcus kodakarensis has two functional PCNA homologs but only one is required for viability.Extremophiles : life under extreme conditions · 2013Article
- Genetic studies on the virus-like regions in the genome of hyperthermophilic archaeon, Thermococcus kodakarensis.Extremophiles : life under extreme conditions · 2013Article
- Characterization of DNA primase complex isolated from the archaeon, Thermococcus kodakaraensis.The Journal of biological chemistry · 2012Article
- Rings in the extreme: PCNA interactions and adaptations in the archaea.Archaea (Vancouver, B.C.) · 2012Review
- Thermococcus kodakarensis encodes three MCM homologs but only one is essential.Nucleic acids research · 2011Article
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
Proliferating cell nuclear antigen (PCNA) is a ring-shaped protein that encircles duplex DNA and plays an essential role in many DNA metabolic processes in archaea and eukarya. The eukaryotic and euryarchaea genomes contain a single gene encoding for PCNA. Interestingly, the genome of the euryarchaeon Thermococcus kodakaraensis contains two PCNA-encoding genes (TK0535 and TK0582), making it unique among the euryarchaea kingdom. It is shown here that the two T. kodakaraensis PCNA proteins support processive DNA synthesis by the polymerase. Both proteins form trimeric structures with characteristics similar to those of other archaeal and eukaryal PCNA proteins. One of the notable differences between the TK0535 and TK0582 rings is that the interfaces are different, resulting in different stabilities for the two trimers. The possible implications of these observations for PCNA functions are discussed.
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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.