Pathways for Holliday Junction Processing during Homologous Recombination in Saccharomyces cerevisiae
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Pathways for Holliday Junction Processing during Homologous Recombination in Saccharomyces cerevisiae. / Ashton, Thomas M; Mankouri, Hocine W; Heidenblut, Anna; McHugh, Peter J; Hickson, Ian D.
In: Molecular and Cellular Biology, Vol. 31, No. 9, 01.05.2011, p. 1921-33.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Pathways for Holliday Junction Processing during Homologous Recombination in Saccharomyces cerevisiae
AU - Ashton, Thomas M
AU - Mankouri, Hocine W
AU - Heidenblut, Anna
AU - McHugh, Peter J
AU - Hickson, Ian D
PY - 2011/5/1
Y1 - 2011/5/1
N2 - The Saccharomyces cerevisiae Rmi1 protein is a component of the highly conserved Sgs1-Top3-Rmi1 complex. Deletion of SGS1, TOP3, or RMI1 is synthetically lethal when combined with the loss of the Mus81-Mms4 or Slx1-Slx4 endonucleases, which have been implicated in Holliday junction (HJ) resolution. To investigate the causes of this synthetic lethality, we isolated a temperature-sensitive mutant of the RMI1 strain, referred to as the rmi1-1 mutant. At the restrictive temperature, this mutant phenocopies an rmi1¿ strain but behaves like the wild type at the permissive temperature. Following a transient exposure to methyl methanesulfonate, rmi1-1 mutants accumulate unprocessed homologous recombination repair (HRR) intermediates. These intermediates are slowly resolved at the restrictive temperature, revealing a redundant resolution activity when Rmi1 is impaired. This resolution depends on Mus81-Mms4 but not on either Slx1-Slx4 or another HJ resolvase, Yen1. Similar results were also observed when Top3 function was impaired. We propose that the Sgs1-Top3-Rmi1 complex constitutes the main pathway for the processing of HJ-containing HRR intermediates but that Mus81-Mms4 can also resolve these intermediates.
AB - The Saccharomyces cerevisiae Rmi1 protein is a component of the highly conserved Sgs1-Top3-Rmi1 complex. Deletion of SGS1, TOP3, or RMI1 is synthetically lethal when combined with the loss of the Mus81-Mms4 or Slx1-Slx4 endonucleases, which have been implicated in Holliday junction (HJ) resolution. To investigate the causes of this synthetic lethality, we isolated a temperature-sensitive mutant of the RMI1 strain, referred to as the rmi1-1 mutant. At the restrictive temperature, this mutant phenocopies an rmi1¿ strain but behaves like the wild type at the permissive temperature. Following a transient exposure to methyl methanesulfonate, rmi1-1 mutants accumulate unprocessed homologous recombination repair (HRR) intermediates. These intermediates are slowly resolved at the restrictive temperature, revealing a redundant resolution activity when Rmi1 is impaired. This resolution depends on Mus81-Mms4 but not on either Slx1-Slx4 or another HJ resolvase, Yen1. Similar results were also observed when Top3 function was impaired. We propose that the Sgs1-Top3-Rmi1 complex constitutes the main pathway for the processing of HJ-containing HRR intermediates but that Mus81-Mms4 can also resolve these intermediates.
U2 - 10.1128/MCB.01130-10
DO - 10.1128/MCB.01130-10
M3 - Journal article
C2 - 21343337
VL - 31
SP - 1921
EP - 1933
JO - Molecular and Cellular Biology
JF - Molecular and Cellular Biology
SN - 0270-7306
IS - 9
ER -
ID: 33489754