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*

*この研究の対応する著者

研究成果: Article査読

8 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)3387-3391
ページ数5
ジャーナルNucleic Acids Research
22
16
出版ステータスPublished - 1994 8 25
外部発表はい

ASJC Scopus subject areas

  • 遺伝学
  • 統計学、確率および不確実性
  • 応用数学
  • 健康、毒物学および変異誘発
  • 毒物学
  • 遺伝学(臨床)

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