p53 Binds Single-Stranded DNA Ends and Catalyzes DNA Renaturation and Strand Transfer

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-t...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1994-01, Vol.91 (1), p.413-417
Main Authors: Bakalkin, Georgy, Yakovleva, Tatjana, Selivanova, Galina, Magnusson, Kristinn P., Szekely, Laszlo, Kiseleva, Elena, Klein, George, Terenius, Lars, Wiman, Klas G.
Format: Article
Language:English
Subjects:
Antibodies
Base Sequence
Biochemistry
Biological and medical sciences
Deoxyribonucleic acid
DNA
DNA damage
DNA Repair
DNA, Single-Stranded - metabolism
DNA-Binding Proteins - metabolism
Fundamental and applied biological sciences. Psychology
Gels
Humans
In Vitro Techniques
Microscopy, Electron
Molecular and cellular biology
Molecular genetics
Molecular Sequence Data
Molecules
Mutagenesis. Repair
Nucleic Acid Renaturation
Oligodeoxyribonucleotides - chemistry
Oligonucleotides
Oncogenes
Plasmids
Proteins
Recombinant Proteins
Single stranded DNA
Tumor Suppressor Protein p53 - metabolism
Tumors
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Summary: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 (≥ 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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.91.1.413