Holliday junction binding activity of the human Rad51B protein

Hiroshi Yokoyama, Hitoshi Kurumizaka, Shukuko Ikawa, Shigeyuki Yokoyama*, Takehiko Shibata

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

53 Citations (Scopus)


The human Rad51B protein is involved in the recombinational repair of damaged DNA. Chromosomal rearrangements of the Rad51B gene have been found in uterine leiomyoma patients, suggesting that the Rad51B gene suppresses tumorigenesis. In the present study, we found that the purified Rad51B protein bound to single-stranded DNA and double-stranded DNA in the presence of ATP and either Mg2+ or Mn2+ and hydrolyzed ATP in a DNA-dependent manner. When the synthetic Holliday junction was present along with the half-cruciform and double-stranded oligonucleotides, the Rad51B protein only bound to the synthetic Holliday junction, which mimics a key intermediate in homologous recombination. In contrast, the human Rad51 protein bound to all three DNA substrates with no obvious preference. Therefore, the Rad51B protein may have a specific function in Holliday junction processing in the homologous recombinational repair pathway in humans.

Original languageEnglish
Pages (from-to)2767-2772
Number of pages6
JournalJournal of Biological Chemistry
Issue number4
Publication statusPublished - 2003 Jan 24
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry


Dive into the research topics of 'Holliday junction binding activity of the human Rad51B protein'. Together they form a unique fingerprint.

Cite this