Specific defects in double-stranded DNA unwinding and homologous pairing of a mutant RecA protein

Hitoshi Kurumizaka*, Hideki Aihara, Shukuko Ikawa, 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 DNA molecules bound to RecA filaments are extended 1.5-fold relative to B-form DNA. This extended DNA structure may be important in the recognition of homology between single-stranded DNA (ssDNA) and double-stranded DNA (dsDNA). In this study, we show that the K286N mutation specifically impaired the dsDNA unwinding and homologous pairing activities of RecA, without an apparent effect on dsDNA binding itself. In contrast, the R243Q mutation caused defective dsDNA unwinding, due to the defective dsDNA binding of the C-terminal domain of RecA. These results provide new evidence that dsDNA unwinding is essential to homology recognition between ssDNA and dsDNA during homologous pairing. Copyright (C) 2000 Federation of European Biochemical Societies.

本文言語English
ページ(範囲)129-134
ページ数6
ジャーナルFEBS Letters
477
1-2
DOI
出版ステータスPublished - 2000 7月 14
外部発表はい

ASJC Scopus subject areas

  • 生化学
  • 生物理学
  • 分子生物学

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