ArticleNucleic acids research2002
Physical and functional interactions of the tumor suppressor protein p53 and DNA polymerase alpha-primase.
Article in Nucleic acids research, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
12 citing papers in PubMed, 33 citations in OpenAlex.
- Canonical and non-canonical functions of p53 isoforms: potentiating the complexity of tumor development and therapy resistance.Cell death & disease · 2024Review
- SV40 T antigen helicase domain regions responsible for oligomerisation regulate Okazaki fragment synthesis initiation.FEBS open bio · 2022Article
- Alkoxylalkyl Esters of Nucleotide Analogs Inhibit Polyomavirus DNA Replication and Large T Antigen Activities.Antimicrobial agents and chemotherapy · 2021Article
- Fidelity of DNA replication-a matter of proofreading.Current genetics · 2018Review
- Review
- DNA damage tolerance pathway involving DNA polymerase ι and the tumor suppressor p53 regulates DNA replication fork progression.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Human cytomegalovirus primase UL70 specifically interacts with cellular factor Snapin.Journal of virology · 2011Article
- Exonucleolytic degradation of RNA by p53 protein in cytoplasm.Journal of molecular medicine (Berlin, Germany) · 2008Article
- Excision of nucleoside analogs from DNA by p53 protein, a potential cellular mechanism of resistance to inhibitors of human immunodeficiency virus type 1 reverse transcriptase.Antimicrobial agents and chemotherapy · 2005Article
- P53 in cytoplasm may enhance the accuracy of DNA synthesis by human immunodeficiency virus type 1 reverse transcriptase.Oncogene · 2004Article
- p53 mutated in the transactivation domain retains regulatory functions in homology-directed double-strand break repair.Oncogene · 2003Article
- p53-associated 3'-->5' exonuclease activity in nuclear and cytoplasmic compartments of cells.Oncogene · 2003Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The wild-type form of p53 contains an intrinsic 3'-5'-exonuclease activity. As p53 forms a complex with DNA polymerase alpha-primase (pol-prim) in vivo this finding suggests that p53 might cooperate with pol-prim to stabilize the genetic information of living cells. To test this hypothesis, exonuclease-free DNA pol-prim was expressed alone or together with p53 for purification. Pol-prim formed a complex with p53, which was purified by ion exchange and immunoaffinity chromatography from baculovirus-infected insect cells. The p53-containing pol-prim fractions removed a 3'-unpaired nucleotide with a 1.5-2-fold higher rate than a paired nucleotide, whereas the four subunit pol-prim did not have any exonuclase activity. Therefore, only p53/pol-prim was able to elongate a primer-template that contained a 3'-unpaired primer end in vitro. To achieve this, the 3'-5'-exonuclease activity of p53 excised the unpaired nucleotide at the 3'-end of the primer and created a paired 3'-end, which pol-prim was able to elongate. The exonuclease activity of p53 as well as the elongation of a primer with a mispaired 3'-end was inhibited specifically by the anti-p53 monoclonal antibodies PAb240 and PAb421.
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Registered trials
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