دورية
An Epistasis Analysis of recAand recNin Escherichia coliK-12
| العنوان: | An Epistasis Analysis of recAand recNin Escherichia coliK-12 |
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| المؤلفون: | Klimova, Anastasiia N, Sandler, Steven J |
| المصدر: | Genetics; October 2020, Vol. 216 Issue: 2 p381-393, 13p |
| مستخلص: | RecA is essential for double-strand-break repair (DSBR) and the SOS response in Escherichia coliK-12. RecN is an SOS protein and a member of the Structural Maintenance of Chromosomes family of proteins thought to play a role in sister chromatid cohesion/interactions during DSBR. Previous studies have shown that a plasmid-encoded recA4190(Q300R) mutant had a phenotype similar to ∆recN(mitomycin C sensitive and UV resistant). It was hypothesized that RecN and RecA physically interact, and that recA4190specifically eliminated this interaction. To test this model, an epistasis analysis between recA4190and ∆recNwas performed in wild-type and recBC sbcBCcells. To do this, recA4190was first transferred to the chromosome. As single mutants, recA4190and ∆recNwere Rec+as measured by transductional recombination, but were 3-fold and 10-fold decreased in their ability to do I-SceI-induced DSBR, respectively. In both cases, the double mutant had an additive phenotype relative to either single mutant. In the recBC sbcBCbackground, recA4190and ∆recNcells were very UVS(sensitive), Rec−, had high basal levels of SOS expression and an altered distribution of RecA-GFP structures. In all cases, the double mutant had additive phenotypes. These data suggest that recA4190(Q300R) and ∆recNremove functions in genetically distinct pathways important for DNA repair, and that RecA Q300 was not important for an interaction between RecN and RecA in vivo. recA4190(Q300R) revealed modest phenotypes in a wild-type background and dramatic phenotypes in a recBC sbcBCstrain, reflecting greater stringency of RecA’s role in that background. |
| قاعدة البيانات: | Supplemental Index |
Full Text Finder | تدمد: | 00166731 19432631 |
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| DOI: | 10.1534/genetics.120.303476 |