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

Hitoshi Kurumizaka, Hideki Aihara, Shukuko Ikawa, Takehiko Shibata

Research output: Contribution to journalArticlepeer-review

8 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)129-134
Number of pages6
JournalFEBS Letters
Issue number1-2
StatePublished - Jul 14 2000

Bibliographical note

Funding Information:
We thank W. Kagawa for critical reading of this manuscript. This work was supported by the Biodesign Research Program (RIKEN), CREST of JST, and also by a Grant-in-Aid from the Ministry of Education, Science, Sports, and Culture, Japan.

Copyright 2007 Elsevier B.V., All rights reserved.


  • DNA binding
  • DNA unwinding
  • Homologous pairing
  • RecA
  • RecA mutant
  • Recombination


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