The RecQ helicase-topoisomerase III-Rmi1 complex: a DNA structure-specific 'dissolvasome'?

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The RecQ helicase-topoisomerase III-Rmi1 complex: a DNA structure-specific 'dissolvasome'? / Mankouri, Hocine W; Hickson, Ian D.

In: Trends in Biochemical Sciences, Vol. 32, No. 12, 01.12.2007, p. 538-46.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Mankouri, HW & Hickson, ID 2007, 'The RecQ helicase-topoisomerase III-Rmi1 complex: a DNA structure-specific 'dissolvasome'?', Trends in Biochemical Sciences, vol. 32, no. 12, pp. 538-46. https://doi.org/10.1016/j.tibs.2007.09.009

APA

Mankouri, H. W., & Hickson, I. D. (2007). The RecQ helicase-topoisomerase III-Rmi1 complex: a DNA structure-specific 'dissolvasome'? Trends in Biochemical Sciences, 32(12), 538-46. https://doi.org/10.1016/j.tibs.2007.09.009

Vancouver

Mankouri HW, Hickson ID. The RecQ helicase-topoisomerase III-Rmi1 complex: a DNA structure-specific 'dissolvasome'? Trends in Biochemical Sciences. 2007 Dec 1;32(12):538-46. https://doi.org/10.1016/j.tibs.2007.09.009

Author

Mankouri, Hocine W ; Hickson, Ian D. / The RecQ helicase-topoisomerase III-Rmi1 complex: a DNA structure-specific 'dissolvasome'?. In: Trends in Biochemical Sciences. 2007 ; Vol. 32, No. 12. pp. 538-46.

Bibtex

@article{aea6bc46ace14658a8926fab497122ab,
title = "The RecQ helicase-topoisomerase III-Rmi1 complex: a DNA structure-specific 'dissolvasome'?",
abstract = "RecQ helicases, together with topoisomerase III and Rmi1 family proteins, form an evolutionarily conserved complex that is essential for the maintenance of genome integrity. This complex, which we term RTR, is capable of, or has been implicated in, the processing of a diverse array of DNA structures, and we propose here that it functions in a coordinated fashion as a DNA structure-specific 'dissolvasome'. Little is known about how the RTR complex might be regulated or targeted to various DNA structures in vivo. Recent findings indicate that the components of the RTR complex might activate the cell cycle checkpoint machinery as well as be a target of checkpoint kinases, suggesting that these events are crucial to ensure faithful DNA replication and chromosome segregation.",
keywords = "DNA Topoisomerases, Type I, DNA, Fungal, DNA-Binding Proteins, Nucleic Acid Conformation, RecQ Helicases, Saccharomyces cerevisiae Proteins, Signal Transduction",
author = "Mankouri, {Hocine W} and Hickson, {Ian D}",
year = "2007",
month = dec,
day = "1",
doi = "10.1016/j.tibs.2007.09.009",
language = "English",
volume = "32",
pages = "538--46",
journal = "Trends in Biochemical Sciences",
issn = "0968-0004",
publisher = "Elsevier",
number = "12",

}

RIS

TY - JOUR

T1 - The RecQ helicase-topoisomerase III-Rmi1 complex: a DNA structure-specific 'dissolvasome'?

AU - Mankouri, Hocine W

AU - Hickson, Ian D

PY - 2007/12/1

Y1 - 2007/12/1

N2 - RecQ helicases, together with topoisomerase III and Rmi1 family proteins, form an evolutionarily conserved complex that is essential for the maintenance of genome integrity. This complex, which we term RTR, is capable of, or has been implicated in, the processing of a diverse array of DNA structures, and we propose here that it functions in a coordinated fashion as a DNA structure-specific 'dissolvasome'. Little is known about how the RTR complex might be regulated or targeted to various DNA structures in vivo. Recent findings indicate that the components of the RTR complex might activate the cell cycle checkpoint machinery as well as be a target of checkpoint kinases, suggesting that these events are crucial to ensure faithful DNA replication and chromosome segregation.

AB - RecQ helicases, together with topoisomerase III and Rmi1 family proteins, form an evolutionarily conserved complex that is essential for the maintenance of genome integrity. This complex, which we term RTR, is capable of, or has been implicated in, the processing of a diverse array of DNA structures, and we propose here that it functions in a coordinated fashion as a DNA structure-specific 'dissolvasome'. Little is known about how the RTR complex might be regulated or targeted to various DNA structures in vivo. Recent findings indicate that the components of the RTR complex might activate the cell cycle checkpoint machinery as well as be a target of checkpoint kinases, suggesting that these events are crucial to ensure faithful DNA replication and chromosome segregation.

KW - DNA Topoisomerases, Type I

KW - DNA, Fungal

KW - DNA-Binding Proteins

KW - Nucleic Acid Conformation

KW - RecQ Helicases

KW - Saccharomyces cerevisiae Proteins

KW - Signal Transduction

U2 - 10.1016/j.tibs.2007.09.009

DO - 10.1016/j.tibs.2007.09.009

M3 - Journal article

C2 - 17980605

VL - 32

SP - 538

EP - 546

JO - Trends in Biochemical Sciences

JF - Trends in Biochemical Sciences

SN - 0968-0004

IS - 12

ER -

ID: 33752849