A chimeric Rec-A protein that implicates non-Watson - Crick interactions in homologous pairing

Hitoshi Kurumizaka, B. J. Rao, Tomoko Ogawa, Charles M. Radding, Takehiko Shibata

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Abstract

The helical filament formed by RecA protein on single-stranded DNA plays an important role in homologous recombination and pairs with a complementary single strand or homologous duplex DNA. The RecA nucleoprotein filament also recognizes an identical single strand. The chimeric protein, RecAc38, forms a nucleoprotein filament that recognizes a complementary strand but is defective in recognition of duplex DNA, and is associated with phenotypic defects in repair and recombination. As described here, RecAc38 nucleoprotein filament is also defective in recognition of an identical strand, either when the filament has within it a single strand or duplex DNA. A model that postulates three DNA binding sites rationalizes these observations and suggests that the third binding site mediates non-Watson-Crick interactions that are instrumental in recognition of homology in duplex DNA.

Original languageEnglish
Pages (from-to)3387-3391
Number of pages5
JournalNucleic Acids Research
Volume22
Issue number16
Publication statusPublished - 1994 Aug 25
Externally publishedYes

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ASJC Scopus subject areas

  • Genetics
  • Statistics, Probability and Uncertainty
  • Applied Mathematics
  • Health, Toxicology and Mutagenesis
  • Toxicology
  • Genetics(clinical)

Cite this

Kurumizaka, H., Rao, B. J., Ogawa, T., Radding, C. M., & Shibata, T. (1994). A chimeric Rec-A protein that implicates non-Watson - Crick interactions in homologous pairing. Nucleic Acids Research, 22(16), 3387-3391.