Electron microscopic single particle analysis of a tetrameric RuvA/RuvB/Holliday junction DNA complex

Kouta Mayanagi, Yoshie Fujiwara, Tomoko Miyata, Kosuke Morikawa

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

During the late stage of homologous recombination in prokaryotes, RuvA binds to the Holliday junction intermediate and executes branch migration in association with RuvB. The RuvA subunits form two distinct complexes with the Holliday junction: complex I with the single RuvA tetramer on one side of the four way junction DNA, and complex II with two tetramers on both sides. To investigate the functional roles of complexes I and II, we mutated two residues of RuvA (L125D and E126K) to prevent octamer formation. An electron microscopic analysis indicated that the mutant RuvA/RuvB/Holliday junction DNA complex formed the characteristic tripartite structure, with only one RuvA tetramer bound to one side of the Holliday junction, demonstrating the unexpected stability of this complex. The novel bent images of the complex revealed an intriguing morphological similarity to the structure of SV40 large T antigen, which belongs to the same AAA+ family as RuvB.

Original languageEnglish
Pages (from-to)273-278
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume365
Issue number2
DOIs
Publication statusPublished - Jan 11 2008
Externally publishedYes

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Cruciform DNA
Electrons
Viral Tumor Antigens
DNA
Polyomavirus Transforming Antigens
Homologous Recombination

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Electron microscopic single particle analysis of a tetrameric RuvA/RuvB/Holliday junction DNA complex. / Mayanagi, Kouta; Fujiwara, Yoshie; Miyata, Tomoko; Morikawa, Kosuke.

In: Biochemical and Biophysical Research Communications, Vol. 365, No. 2, 11.01.2008, p. 273-278.

Research output: Contribution to journalArticle

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