ArticleNucleic acids research2009
Physical and functional interactions between human mitochondrial single-stranded DNA-binding protein and tumour suppressor p53.
Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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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
50 citing papers in PubMed, 98 citations in OpenAlex.
- Characterization of Tumor Microenvironment and Prognosis of Regulatory T cells-Related Subtypes.Current medicinal chemistry · 2026Article
- Review
- The complexity of p53-mediated metabolic regulation in tumor suppression.Seminars in cancer biology · 2022Review
- Identification of SSBP1 as a ferroptosis-related biomarker of glioblastoma based on a novel mitochondria-related gene risk model and in vitro experiments.Journal of translational medicine · 2022Article
- Regulation of p53 Function by Formation of Non-Nuclear Heterologous Protein Complexes.Biomolecules · 2022Review
- p53 is required for nuclear but not mitochondrial DNA damage-induced degeneration.Cell death & disease · 2021Article
- Physical and Functional Interaction of Mitochondrial Single-Stranded DNA-Binding Protein and the Catalytic Subunit of DNA Polymerase Gamma.Frontiers in genetics · 2021Article
- Metabolic functions of the tumor suppressor p53: Implications in normal physiology, metabolic disorders, and cancer.Molecular metabolism · 2020Review
- DNA repair and genomic stability in lungs affected by acute injury.Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2019Review
- Replicative DNA polymerases promote active displacement of SSB proteins during lagging strand synthesis.Nucleic acids research · 2019Article
- A stable tetramer is not the only oligomeric state that mitochondrial single-stranded DNA binding proteins can adopt.The Journal of biological chemistry · 2019Article
- Structural Basis for the Interaction between p53 Transactivation Domain and the Mediator Subunit MED25.Molecules (Basel, Switzerland) · 2018Article
- The mitochondrial single-stranded DNA binding protein from S. cerevisiae, Rim1, does not form stable homo-tetramers and binds DNA as a dimer of dimers.Nucleic acids research · 2018Article
- Emerging Roles of p53 Family Members in Glucose Metabolism.International journal of molecular sciences · 2018Review
- Development of a novel immunoassay to detect interactions with the transactivation domain of p53: application to screening of new drugs.Scientific reports · 2017Article
- The human mitochondrial single-stranded DNA-binding protein displays distinct kinetics and thermodynamics of DNA binding and exchange.The Journal of biological chemistry · 2017Article
- DNA synthesis determines the binding mode of the human mitochondrial single-stranded DNA-binding protein.Nucleic acids research · 2017Article
- p53 in the mitochondria, as a trans-acting protein, provides error-correction activities during the incorporation of non-canonical dUTP into DNA.Oncotarget · 2016Article
- TP53 mutation, mitochondria and cancer.Current opinion in genetics & development · 2016Review
- p53 as guardian of the mitochondrial genome.FEBS letters · 2016Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Single-stranded DNA-binding proteins (SSB) form a class of proteins that bind preferentially single-stranded DNA with high affinity. They are involved in DNA metabolism in all organisms and serve a vital role in replication, recombination and repair of DNA. In this report, we identify human mitochondrial SSB (HmtSSB) as a novel protein-binding partner of tumour suppressor p53, in mitochondria. It binds to the transactivation domain (residues 1-61) of p53 via an extended binding interface, with dissociation constant of 12.7 (+/- 0.7) microM. Unlike most binding partners reported to date, HmtSSB interacts with both TAD1 (residues 1-40) and TAD2 (residues 41-61) subdomains of p53. HmtSSB enhances intrinsic 3'-5' exonuclease activity of p53, particularly in hydrolysing 8-oxo-7,8-dihydro-2'-deoxyguanosine (8-oxodG) present at 3'-end of DNA. Taken together, our data suggest that p53 is involved in DNA repair within mitochondria during oxidative stress. In addition, we characterize HmtSSB binding to ssDNA and p53 N-terminal domain using various biophysical measurements and we propose binding models for both.
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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.