ATP-dependent branch migration of Holliday junctions promoted by the RuvA and RuvB proteins of E. coli

I R Tsaneva, Berndt Marino Muller, S C West

Research output: Contribution to journalArticle

202 Citations (Scopus)

Abstract

The RuvA and RuvB proteins of E. coli, which are induced as part of the cellular response to DNA damage, act together to promote the branch migration of Holliday junctions. Addition of purified RuvA and RuvB to a RecA-mediated recombination reaction stimulates the rate of strand exchange and the formation of hetero-duplex DNA. Stimulation does not occur via interaction with RecA; instead, RuvA and RuvB act directly upon recombination intermediates (Holliday junctions) made by RecA. We show that RuvAB-mediated branch migration requires ATP and can bypass UV-induced DNA lesions. At high RuvB concentrations, the requirement for RuvA is overcome, indicating that the RuvB ATPase provides the motor force for branch migration. RuvA protein provides specificity by binding to the Holliday junction, thereby reducing the requirement for RuvB by 50-fold. The newly discovered biochemical properties of RuvA, RuvB, and RuvC are incorporated into a model for the postreplicational repair of DNA following UV irradiation.
Original languageEnglish
Pages (from-to)1171-1180
Number of pages10
JournalCell
Volume69
Issue number7
DOIs
Publication statusPublished - 26 Jun 1992

Fingerprint

Cruciform DNA
Escherichia coli Proteins
Adenosine Triphosphate
Genetic Recombination
DNA
DNA Repair
DNA Damage
Adenosine Triphosphatases
Repair
Irradiation
E coli Holliday junction DNA helicase
Proteins

Keywords

  • Adenosine Triphosphate
  • Bacterial Proteins
  • DNA
  • DNA Damage
  • DNA Helicases
  • DNA Repair
  • DNA-Binding Proteins
  • Escherichia coli
  • Escherichia coli Proteins
  • Models, Molecular
  • Recombination, Genetic

Cite this

ATP-dependent branch migration of Holliday junctions promoted by the RuvA and RuvB proteins of E. coli. / Tsaneva, I R; Muller, Berndt Marino; West, S C.

In: Cell, Vol. 69, No. 7, 26.06.1992, p. 1171-1180.

Research output: Contribution to journalArticle

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abstract = "The RuvA and RuvB proteins of E. coli, which are induced as part of the cellular response to DNA damage, act together to promote the branch migration of Holliday junctions. Addition of purified RuvA and RuvB to a RecA-mediated recombination reaction stimulates the rate of strand exchange and the formation of hetero-duplex DNA. Stimulation does not occur via interaction with RecA; instead, RuvA and RuvB act directly upon recombination intermediates (Holliday junctions) made by RecA. We show that RuvAB-mediated branch migration requires ATP and can bypass UV-induced DNA lesions. At high RuvB concentrations, the requirement for RuvA is overcome, indicating that the RuvB ATPase provides the motor force for branch migration. RuvA protein provides specificity by binding to the Holliday junction, thereby reducing the requirement for RuvB by 50-fold. The newly discovered biochemical properties of RuvA, RuvB, and RuvC are incorporated into a model for the postreplicational repair of DNA following UV irradiation.",
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AU - Tsaneva, I R

AU - Muller, Berndt Marino

AU - West, S C

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Y1 - 1992/6/26

N2 - The RuvA and RuvB proteins of E. coli, which are induced as part of the cellular response to DNA damage, act together to promote the branch migration of Holliday junctions. Addition of purified RuvA and RuvB to a RecA-mediated recombination reaction stimulates the rate of strand exchange and the formation of hetero-duplex DNA. Stimulation does not occur via interaction with RecA; instead, RuvA and RuvB act directly upon recombination intermediates (Holliday junctions) made by RecA. We show that RuvAB-mediated branch migration requires ATP and can bypass UV-induced DNA lesions. At high RuvB concentrations, the requirement for RuvA is overcome, indicating that the RuvB ATPase provides the motor force for branch migration. RuvA protein provides specificity by binding to the Holliday junction, thereby reducing the requirement for RuvB by 50-fold. The newly discovered biochemical properties of RuvA, RuvB, and RuvC are incorporated into a model for the postreplicational repair of DNA following UV irradiation.

AB - The RuvA and RuvB proteins of E. coli, which are induced as part of the cellular response to DNA damage, act together to promote the branch migration of Holliday junctions. Addition of purified RuvA and RuvB to a RecA-mediated recombination reaction stimulates the rate of strand exchange and the formation of hetero-duplex DNA. Stimulation does not occur via interaction with RecA; instead, RuvA and RuvB act directly upon recombination intermediates (Holliday junctions) made by RecA. We show that RuvAB-mediated branch migration requires ATP and can bypass UV-induced DNA lesions. At high RuvB concentrations, the requirement for RuvA is overcome, indicating that the RuvB ATPase provides the motor force for branch migration. RuvA protein provides specificity by binding to the Holliday junction, thereby reducing the requirement for RuvB by 50-fold. The newly discovered biochemical properties of RuvA, RuvB, and RuvC are incorporated into a model for the postreplicational repair of DNA following UV irradiation.

KW - Adenosine Triphosphate

KW - Bacterial Proteins

KW - DNA

KW - DNA Damage

KW - DNA Helicases

KW - DNA Repair

KW - DNA-Binding Proteins

KW - Escherichia coli

KW - Escherichia coli Proteins

KW - Models, Molecular

KW - Recombination, Genetic

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