The Dissolution of Double Holliday Junctions

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The Dissolution of Double Holliday Junctions

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The Dissolution of Double Holliday Junctions. / Bizard, Anna H; Hickson, Ian D.

In: Cold Spring Harbor perspectives in biology, Vol. 6, a016477, 01.07.2014, p. 1-16.

Research output: Contribution to journal › Review › Research › peer-review

Harvard

Bizard, AH & Hickson, ID 2014, 'The Dissolution of Double Holliday Junctions', Cold Spring Harbor perspectives in biology, vol. 6, a016477, pp. 1-16. https://doi.org/10.1101/cshperspect.a016477

APA

Bizard, A. H., & Hickson, I. D. (2014). The Dissolution of Double Holliday Junctions. Cold Spring Harbor perspectives in biology, 6, 1-16. [a016477]. https://doi.org/10.1101/cshperspect.a016477

Vancouver

Bizard AH, Hickson ID. The Dissolution of Double Holliday Junctions. Cold Spring Harbor perspectives in biology. 2014 Jul 1;6:1-16. a016477. https://doi.org/10.1101/cshperspect.a016477

Author

Bizard, Anna H ; Hickson, Ian D. / The Dissolution of Double Holliday Junctions. In: Cold Spring Harbor perspectives in biology. 2014 ; Vol. 6. pp. 1-16.

Bibtex

@article{08db6c4c0bb44065b9bcd591fecfaaec,

title = "The Dissolution of Double Holliday Junctions",

abstract = "Double Holliday junctions (dHJS) are important intermediates of homologous recombination. The separate junctions can each be cleaved by DNA structure-selective endonucleases known as Holliday junction resolvases. Alternatively, double Holliday junctions can be processed by a reaction known as {"}double Holliday junction dissolution.{"} This reaction requires the cooperative action of a so-called {"}dissolvasome{"} comprising a Holliday junction branch migration enzyme (Sgs1/BLM RecQ helicase) and a type IA topoisomerase (Top3/TopoIIIα) in complex with its OB (oligonucleotide/oligosaccharide binding) fold containing accessory factor (Rmi1). This review details our current knowledge of the dissolution process and the players involved in catalyzing this mechanistically complex means of completing homologous recombination reactions.",

author = "Bizard, {Anna H} and Hickson, {Ian D}",

year = "2014",

month = jul,

day = "1",

doi = "10.1101/cshperspect.a016477",

language = "English",

volume = "6",

pages = "1--16",

journal = "Cold Spring Harbor Perspectives in Biology",

issn = "1943-0264",

publisher = "Cold Spring Harbor Laboratory Press",

}

RIS

TY - JOUR

T1 - The Dissolution of Double Holliday Junctions

AU - Bizard, Anna H

AU - Hickson, Ian D

PY - 2014/7/1

Y1 - 2014/7/1

N2 - Double Holliday junctions (dHJS) are important intermediates of homologous recombination. The separate junctions can each be cleaved by DNA structure-selective endonucleases known as Holliday junction resolvases. Alternatively, double Holliday junctions can be processed by a reaction known as "double Holliday junction dissolution." This reaction requires the cooperative action of a so-called "dissolvasome" comprising a Holliday junction branch migration enzyme (Sgs1/BLM RecQ helicase) and a type IA topoisomerase (Top3/TopoIIIα) in complex with its OB (oligonucleotide/oligosaccharide binding) fold containing accessory factor (Rmi1). This review details our current knowledge of the dissolution process and the players involved in catalyzing this mechanistically complex means of completing homologous recombination reactions.

AB - Double Holliday junctions (dHJS) are important intermediates of homologous recombination. The separate junctions can each be cleaved by DNA structure-selective endonucleases known as Holliday junction resolvases. Alternatively, double Holliday junctions can be processed by a reaction known as "double Holliday junction dissolution." This reaction requires the cooperative action of a so-called "dissolvasome" comprising a Holliday junction branch migration enzyme (Sgs1/BLM RecQ helicase) and a type IA topoisomerase (Top3/TopoIIIα) in complex with its OB (oligonucleotide/oligosaccharide binding) fold containing accessory factor (Rmi1). This review details our current knowledge of the dissolution process and the players involved in catalyzing this mechanistically complex means of completing homologous recombination reactions.

U2 - 10.1101/cshperspect.a016477

DO - 10.1101/cshperspect.a016477

M3 - Review

C2 - 24984776

VL - 6

SP - 1

EP - 16

JO - Cold Spring Harbor Perspectives in Biology

JF - Cold Spring Harbor Perspectives in Biology

SN - 1943-0264

M1 - a016477

ER -

ID: 119170260