Functional significance of octameric RuvA for a branch migration complex from Thermus thermophilus

Yoshie Fujiwara, Kouta Mayanagi, Kosuke Morikawa

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

The RuvAB complex promotes migration of Holliday junction at the late stage of homologous recombination. The RuvA tetramer specifically recognizes Holliday junction to form two types of complexes. A single tetramer is bound to the open configuration of the junction DNA in complex I, while the octameric RuvA core structure sandwiches the same junction in complex II. The hexameric RuvB rings, symmetrically bound to both sides of RuvA on Holliday junction, pump out DNA duplexes, depending upon ATP hydrolysis. We investigated functional differences between the wild-type RuvA from Thermus thermophilus and mutants impaired the ability of complex II formation. These mutant RuvA, exclusively forming complex I, reduced activities of branch migration and ATP hydrolysis, suggesting that the octameric RuvA is essential for efficient branch migration. Together with our recent electron microscopic analysis, this finding provides important insights into functional roles of complex II in the coordinated branch migration mechanism.

Original languageEnglish
Pages (from-to)426-431
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume366
Issue number2
DOIs
Publication statusPublished - Feb 8 2008
Externally publishedYes

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Cruciform DNA
Thermus thermophilus
Hydrolysis
Adenosine Triphosphate
Sandwich structures
DNA
Homologous Recombination
Pumps
Electrons

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Functional significance of octameric RuvA for a branch migration complex from Thermus thermophilus. / Fujiwara, Yoshie; Mayanagi, Kouta; Morikawa, Kosuke.

In: Biochemical and Biophysical Research Communications, Vol. 366, No. 2, 08.02.2008, p. 426-431.

Research output: Contribution to journalArticle

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