(Q27765700)

2

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T Brown

3

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M Oram

4

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A Keeley

5

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I R Tsaneva

6

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L H Pearl

Bypass of DNA heterologies during RuvAB-mediated three- and four-strand branch migration.

7

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publication date

September 1998

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published in

Molecular Cell

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volume

2

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issue

3

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page(s)

361-72

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cites work

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Purification of synthetic DNA

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Molecular Mechanisms in Genetic Recombination

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Structure of the four-way DNA junction and its interaction with proteins.

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Formation and resolution of recombination intermediates by E. coli RecA and RuvC proteins.

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In vitro reconstitution of the late steps of genetic recombination in E. coli.

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Branch migration during homologous recombination: assembly of a RuvAB-Holliday junction complex in vitro.

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Molecular analysis of the Pseudomonas aeruginosa genes, ruvA, ruvB and ruvC, involved in processing of homologous recombination intermediates.

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A mechanism for gene conversion in fungi

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Escherichia coli RuvA and RuvB proteins specifically interact with Holliday junctions and promote branch migration

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Blocked RecA protein-mediated DNA strand exchange reactions are reversed by the RuvA and RuvB proteins

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SOS-inducible DNA repair proteins, RuvA and RuvB, of Escherichia coli: functional interactions between RuvA and RuvB for ATP hydrolysis and renaturation of the cruciform structure in supercoiled DNA

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The Escherichia coli RuvB branch migration protein forms double hexameric rings around DNA.

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RuvA and RuvB proteins of Escherichia coli exhibit DNA helicase activity in vitro

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The RecA hexamer is a structural homologue of ring helicases

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Structure and subunit composition of theRuvAB-holliday junction complex 1 1Edited by P. E. Wright

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