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Title 

The tumor suppressor homolog in fission yeast, myh1+, displays a strong interaction with the checkpoint gene rad1+

Authors 

K JanssonJ WarringerA FarewellH O ParkKwang Lae HoeDong Uk KimJ HaylesP Sunnerhagen

Issue Date 

2008

Citation 

Mutation Res-Fund Mol M, vol. 644, no. 1, pp. 48-55

Keywords 

9-1-1 complexBase-excision repairDNA glycosylaseDNA repairUV sensitivityhydroxyureaDNA damagegenegene interactionmyh1 gene

Abstract 

The DNA glycosylase MutY is strongly conserved in evolution, and homologs are found in most eukaryotes and prokaryotes examined. This protein is implicated in repair of oxidative DNA damage, in particular adenine mispaired opposite 7,8-dihydro-8-oxoguanine. Previous investigations in Escherichia coli, fission yeast, and mammalian cells show an association of mutations in MutY homologs with a mutator phenotype and carcinogenesis. Eukaryotic MutY homologs physically associate with several proteins with a role in replication, DNA repair, and checkpoint signaling, specifically the trimeric 9-1-1 complex. In a genetic investigation of the fission yeast MutY homolog, myh1+, we show that the myh1 mutation confers a moderately increased UV sensitivity alone and in combination with mutations in several DNA repair genes. The myh1 rad1, and to a lesser degree myh1 rad9, double mutants display a synthetic interaction resulting in enhanced sensitivity to DNA damaging agents and hydroxyurea. UV irradiation of myh1 rad1 double mutants results in severe chromosome segregation defects and visible DNA fragmentation, and a failure to activate the checkpoint. Additionally, myh1 rad1 double mutants exhibit morphological defects in the absence of DNA damaging agents. We also found a moderate suppression of the slow growth and UV sensitivity of rhp51 mutants by the myh1 mutation. Our results implicate fission yeast Myh1 in repair of a wider range of DNA damage than previously thought, and functionally link it to the checkpoint pathway.

ISSN 

0027-5107

Link 

http://dx.doi.org/10.1016/j.mrfmmm.2008.07.001

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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