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P53 binds single-stranded DNA ends and catalyzes DNA renaturation and strand transfer

Academic Article
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Overview

authors

  • Bakalkin, G.
  • Yakovleva, T.
  • Selivanova, G.
  • Magnusson, K. P.
  • Szekely, L.
  • Kiseleva, E.
  • Klein, G.
  • Terenius, Lars
  • Wiman, K. G.

publication date

  • 1994

journal

  • Proceedings of the National Academy of Sciences of the United States of America  Journal

abstract

  • The p53 tumor-suppressor protein has previously been shown to bind double-stranded and single-stranded DNA. We report that the p53 protein can bind single-stranded DNA ends and catalyze DNA renaturation and DNA strand transfer. Both a bacterially expressed wild-type p53 protein and a glutathione S-transferase-wild-type p53 fusion protein catalyzed renaturation of different short (25- to 76-nt) complementary single-stranded DNA fragments and promoted strand transfer between short (36-bp) duplex DNA and complementary single-stranded DNA. Mutant p53 fusion proteins carrying amino acid substitutions Glu-213, Ile-237, or Tyr-238, derived from mutant p53 genes of Burkitt lymphomas, failed to catalyze these reactions. Wild-type p53 had significantly higher binding affinity for short (36- to 76-nt) than for longer (> or = 462-nt) single-stranded DNA fragments in an electrophoretic mobility-shift assay. Moreover, electron microscopy showed that p53 preferentially binds single-stranded DNA ends. Binding of DNA ends to p53 oligomers may allow alignment of complementary strands. These findings suggest that p53 may play a direct role in the repair of DNA breaks, including the joining of complementary single-stranded DNA ends.

subject areas

  • Base Sequence
  • DNA Repair
  • DNA, Single-Stranded
  • DNA-Binding Proteins
  • Humans
  • In Vitro Techniques
  • Microscopy, Electron
  • Molecular Sequence Data
  • Nucleic Acid Renaturation
  • Oligodeoxyribonucleotides
  • Recombinant Proteins
  • Tumor Suppressor Protein p53
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Research

keywords

  • DNA REPAIR
  • TUMOR-SUPPRESSOR PROTEIN
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Identity

PubMed Central ID

  • PMC42958

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.91.1.413

PubMed ID

  • 8278402
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Additional Document Info

start page

  • 413

end page

  • 417

volume

  • 91

issue

  • 1

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