Processing of homologous recombination repair intermediates by the Sgs1-Top3-Rmi1 and Mus81-Mms4 complexes

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Standard

Processing of homologous recombination repair intermediates by the Sgs1-Top3-Rmi1 and Mus81-Mms4 complexes. / Hickson, Ian D; Mankouri, Hocine W.

In: Cell Cycle, Vol. 10, No. 18, 10.2011, p. 3078-85.

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

Harvard

Hickson, ID & Mankouri, HW 2011, 'Processing of homologous recombination repair intermediates by the Sgs1-Top3-Rmi1 and Mus81-Mms4 complexes', Cell Cycle, vol. 10, no. 18, pp. 3078-85.

APA

Hickson, I. D., & Mankouri, H. W. (2011). Processing of homologous recombination repair intermediates by the Sgs1-Top3-Rmi1 and Mus81-Mms4 complexes. Cell Cycle, 10(18), 3078-85.

Vancouver

Hickson ID, Mankouri HW. Processing of homologous recombination repair intermediates by the Sgs1-Top3-Rmi1 and Mus81-Mms4 complexes. Cell Cycle. 2011 Oct;10(18):3078-85.

Author

Hickson, Ian D ; Mankouri, Hocine W. / Processing of homologous recombination repair intermediates by the Sgs1-Top3-Rmi1 and Mus81-Mms4 complexes. In: Cell Cycle. 2011 ; Vol. 10, No. 18. pp. 3078-85.

Bibtex

@article{de5d9b45783b44d09c7a4c189bef059d,
title = "Processing of homologous recombination repair intermediates by the Sgs1-Top3-Rmi1 and Mus81-Mms4 complexes",
abstract = "Homologous recombination repair (HRR) is an evolutionarily conserved cellular process that is important for the maintenance of genome stability during S phase. Inactivation of the Saccharomyces cerevisiae Sgs1-Top3-Rmi1 complex leads to the accumulation of unprocessed, X-shaped HRR intermediates (X structures) following replicative stress. Further characterization of these X structures may reveal why loss of BLM (the human Sgs1 ortholog) leads to the human cancer predisposition disorder, Bloom syndrome. In two recent complementary studies, we examined the nature of the X structures arising in yeast strains lacking Sgs1, Top3 or Rmi1 by identifying which proteins could process these structures in vivo. We revealed that the unprocessed X structures that accumulate in these strains could be resolved by the ectopic overexpression of two different Holliday junction (HJ) resolvases, and that the endogenous Mus81-Mms4 endonuclease could also remove them, albeit slowly. In this review, we discuss the implications of these results and review the putative roles for the Sgs1-Top3-Rmi1 and Mus81-Mms4 complexes in the processing of various types of HRR intermediates during S phase.",
keywords = "DNA Breaks, Single-Stranded, DNA Replication, DNA, Cruciform, DNA-Binding Proteins, Endonucleases, Holliday Junction Resolvases, Humans, RecQ Helicases, Recombinational DNA Repair, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins",
author = "Hickson, {Ian D} and Mankouri, {Hocine W}",
year = "2011",
month = oct,
language = "English",
volume = "10",
pages = "3078--85",
journal = "Cell Cycle",
issn = "1538-4101",
publisher = "Taylor & Francis",
number = "18",

}

RIS

TY - JOUR

T1 - Processing of homologous recombination repair intermediates by the Sgs1-Top3-Rmi1 and Mus81-Mms4 complexes

AU - Hickson, Ian D

AU - Mankouri, Hocine W

PY - 2011/10

Y1 - 2011/10

N2 - Homologous recombination repair (HRR) is an evolutionarily conserved cellular process that is important for the maintenance of genome stability during S phase. Inactivation of the Saccharomyces cerevisiae Sgs1-Top3-Rmi1 complex leads to the accumulation of unprocessed, X-shaped HRR intermediates (X structures) following replicative stress. Further characterization of these X structures may reveal why loss of BLM (the human Sgs1 ortholog) leads to the human cancer predisposition disorder, Bloom syndrome. In two recent complementary studies, we examined the nature of the X structures arising in yeast strains lacking Sgs1, Top3 or Rmi1 by identifying which proteins could process these structures in vivo. We revealed that the unprocessed X structures that accumulate in these strains could be resolved by the ectopic overexpression of two different Holliday junction (HJ) resolvases, and that the endogenous Mus81-Mms4 endonuclease could also remove them, albeit slowly. In this review, we discuss the implications of these results and review the putative roles for the Sgs1-Top3-Rmi1 and Mus81-Mms4 complexes in the processing of various types of HRR intermediates during S phase.

AB - Homologous recombination repair (HRR) is an evolutionarily conserved cellular process that is important for the maintenance of genome stability during S phase. Inactivation of the Saccharomyces cerevisiae Sgs1-Top3-Rmi1 complex leads to the accumulation of unprocessed, X-shaped HRR intermediates (X structures) following replicative stress. Further characterization of these X structures may reveal why loss of BLM (the human Sgs1 ortholog) leads to the human cancer predisposition disorder, Bloom syndrome. In two recent complementary studies, we examined the nature of the X structures arising in yeast strains lacking Sgs1, Top3 or Rmi1 by identifying which proteins could process these structures in vivo. We revealed that the unprocessed X structures that accumulate in these strains could be resolved by the ectopic overexpression of two different Holliday junction (HJ) resolvases, and that the endogenous Mus81-Mms4 endonuclease could also remove them, albeit slowly. In this review, we discuss the implications of these results and review the putative roles for the Sgs1-Top3-Rmi1 and Mus81-Mms4 complexes in the processing of various types of HRR intermediates during S phase.

KW - DNA Breaks, Single-Stranded

KW - DNA Replication

KW - DNA, Cruciform

KW - DNA-Binding Proteins

KW - Endonucleases

KW - Holliday Junction Resolvases

KW - Humans

KW - RecQ Helicases

KW - Recombinational DNA Repair

KW - Saccharomyces cerevisiae

KW - Saccharomyces cerevisiae Proteins

M3 - Review

C2 - 21876385

VL - 10

SP - 3078

EP - 3085

JO - Cell Cycle

JF - Cell Cycle

SN - 1538-4101

IS - 18

ER -

ID: 38333130