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Cited by 81Cancer-related Molecular PathwaysDNA and Nucleic Acid ChemistryDiffusion and Search Dynamics

The DOI matches its Crossref record; 67 of the 67 references it cites were found in a registry or an index.

High-Affinity Binding of Tumor-Suppressor Protein p53 and HMGB1 to Hemicatenated DNA Loops

Štros, Michal, Muselíková-Polanská, Eva, Pospíšilová, Šárka, Strauss, François·2004·Biochemistry
DOI 10.1021/bi049928k
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Abstract

We have recently observed that chromatin architectural protein HMGB1 (previously reported to be involved in numerous biological processes such as DNA replication, recombination, repair, tumor growth, and metastasis) could bind with extremely high affinity (K(d) < 1 pM) to a novel DNA structure that forms a DNA loop maintained at its base by a hemicatenane (hcDNA). The loop of hcDNA contains a track of repetitive sequences derived from CA-microsatellites. Here, we report using a gel-retardation assay that tumor-suppressor protein p53 can also bind to hcDNA. p53 is a crucial molecule protecting cells from malignant transformation by regulating cell-cycle progression, apoptosis, and DNA repair by activation or repression of transcription of its target genes by binding to specific p53 DNA-binding sites and/or certain types of DNA lesions or alternative DNA structures. The affinity of p53 for hcDNA (containing sequences with no resemblance to the p53 DNA consensus sequence) is >40-fold higher (K(d) approximately 0.5 nM) than that for its natural specific binding sites within its target genes (Mdm2 promoter). Binding of p53 to hcDNA remains detectable in the presence of up to approximately 4 orders of magnitude of mass excess of competitor linear DNA, suggesting a high specificity of the interaction. p53 displays a higher affinity for hcDNA than for DNA minicircles (lacking functional p53-specific binding sequence) with a size similar to that of the loop within the hcDNA, indicating that the extreme affinity of p53 for hcDNA is likely due to the binding of the protein to the hemicatenane. Although binding of p53 to hcDNA occurs in the absence of the nonspecific DNA-binding extreme carboxy-terminal regulatory domain (30-C, residues 363-393), the isolated 30-C domain (but not the sequence-specific p53 "core domain", residues 94-312) can also bind hcDNA. Only the full-length p53 can form stable ternary complexes with hcDNA and HMGB1. The possible biological relevance of p53 and HMGB1 binding to hemicatenanes is discussed.

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Citations

Cites

Research works printed but not linked: 32

  1. Wang X. W., 1996, Cancer Surv. 28, 169−196.
  2. Sturzberger H. W., 1996, EMBO J., 15
  3. Lee S., 1997, J. Biol. Chem., 272
  4. Bakalkin G., 1994, Proc. Natl. Acad. Sci. U.S.A. 91
  5. Thomas J. O., 2001, DNA-binding proteins, Trends Biochem. Sci. 26, 167−174.
  6. Agresti A., 2003, Curr. Opin. Genet. Dev. 13, 170−178.
  7. Jaouen S., 2004, Binding of HMG-box proteins to hemicatenated DNA loops, unpublished results
  8. Štros M., 1994, FEBS Lett., 343
  9. Pospíšilová S., 2003, Biochem. J., 378
  10. Pil P. M., 1992, Science 256, 234−237.
  11. Lyubchenko Y. L., 2002, Nucleic Acids Res. 30, 4902−4909.
  12. Webb M., 2001, J. Mol. Biol., 309, 88
  13. Bianchi M. E., 1989, Science 243, 1056−1059.
  14. Fojta M., 2003, Recognition of DNA modified by antitumor cisplatin by “latent
  15. Imamura T., 2001, J. Biol. Chem., 276
  16. Štros M., 2001, Biochemistry 40, 4769−4779.
  17. Cunningham R. P., 1981, Cell 24, 213−223.
  18. Bianchi M., 1983, Cell 34, 931−939.
  19. Kmiec E. B., 1986, Cell 44, 545−554.
  20. McKee B. D., 1992, Genetics 132, 529−544.
  21. Schwacha A., 1995, Cell 83, 783−791.
  22. Polanco C., 2000, Genetics 155, 1221−1229.
  23. Kajander O. A., 2001, EMBO Rep. 2, 1007−1012.
  24. Segurado M., 2002, Mol. Cells 10, 907−916.
  25. Sogo J. M., 1986, J. Mol. Biol., 189
  26. Lucas I., 2000, Nucleic Acids Res. 28, 2187−2193.
  27. Benard M., 2001, Mol. Cells 7, 971−980.
  28. Wellinger R. E., 2003, Mol. Cell. Biol. 23, 6363−6372.
  29. Rubbi C. P., 2003, EMBO J., 22
  30. Wang L., 2001, J. Biol. Chem., 276
  31. Scaffidi P., 2002, Nature 418, 191−195.
  32. Abbreviations HMG, high-mobility group

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Metadata

Authors
Štros, M., Muselíková-Polanská, E., Pospíšilová, Š., & Strauss, F.
Affiliations
Czech Academy of Sciences, Institute of Biophysics (CZ)
Corresponding author
Štros, Michal
ORCID
Venue
Biochemistry
Publisher
American Chemical Society (ACS)
Published
2004-05-13
Volume
43
Issue
22
Pages
7215-7225
ISSN
  • 0006-2960 (ISSN-L)
  • 1520-4995
DOI
10.1021/bi049928k
OpenAlex
W2085442496
Cited by
81
References
67
Citations by year
2025: 2 · 2024: 1 · 2023: 1 · 2022: 5 · 2021: 2 · 2019: 6 · 2018: 2 · 2017: 4 · 2016: 6 · 2015: 3 · 2014: 5 · 2013: 3 · 2012: 7
FWCI
2.21
Type
journal article
Language
en
Open access
closed
Locations
  • Biochemistry (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA and Nucleic Acid Chemistry
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Diffusion and Search Dynamics
Keywords
p53, HMGB1, DNA loops, alternative DNA structures, protein-DNA binding affinity, chromatin structure, tumor suppressor proteins
MeSH terms
Animals, Binding Sites, Cattle, Glutathione Transferase, Humans, Nucleic Acid Conformation, Promoter Regions, Genetic, Protein Binding, Substrate Specificity, Thymus Gland, Transcriptional Activation, Tumor Suppressor Protein p53, Protein Structure, Tertiary, Electrophoretic Mobility Shift Assay, HMGB1 Protein, Tumor Suppressor Proteins, DNA, Catenated, Rats

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