Reduction of postreplication DNA repair in two Escherichia coli mutants with temperature-sensitive polymerase III activity: implications for the postreplication repair pathway

Johnson, Robert C.

doi:10.1128/jb.136.1.125-130.1978

Cited by 9 publications

(2 citation statements)

References 7 publications

(12 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…We favor the model that Pol III HE is recruited at ssDNA gaps, given the presence of SSB. Polymerization activity at these sites is also likely and agrees with reports that established Pol III activity at ssDNA gaps (42,43). Pol III HE might also contribute to loading of β-clamp at these sites, which could then serve for the recruitment of Pol V translesion polymerase.…”

Section: Discussionsupporting

confidence: 86%

Replisome activity slowdown after exposure to ultraviolet light in Escherichia coli

Soubry

Wang

Reyes‐Lamothe

2019

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

The replisome is a multiprotein machine that is responsible for replicating DNA. During active DNA synthesis, the replisome tightly associates with DNA. In contrast, after DNA damage, the replisome may disassemble, exposing DNA to breaks and threatening cell survival. Using live cell imaging, we studied the effect of UV light on the replisome of Escherichia coli. Surprisingly, our results showed an increase in Pol III holoenzyme (Pol III HE) foci post-UV that do not colocalize with the DnaB helicase. Formation of these foci is independent of active replication forks and dependent on the presence of the χ subunit of the clamp loader, suggesting recruitment of Pol III HE at sites of DNA repair. Our results also showed a decrease of DnaB helicase foci per cell after UV, consistent with the disassembly of a fraction of the replisomes. By labeling newly synthesized DNA, we demonstrated that a drop in the rate of synthesis is not explained by replisome disassembly alone. Instead, we show that most replisomes continue synthesizing DNA at a slower rate after UV. We propose that the slowdown in replisome activity is a strategy to prevent clashes with engaged DNA repair proteins and preserve the integrity of the replication fork.DNA replication | replisome | fluorescence microscopy | UV | Escherichia coli

show abstract

Section: Discussionsupporting

confidence: 86%

Replisome activity slowdown after exposure to ultraviolet light in Escherichia coli

Soubry

Wang

Reyes‐Lamothe

2019

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

show abstract

“…18). Now is the time to mention mutants with mutations in DNA-keeping genes, partially defective in daughter strand gap closure, like uvrD (helicase II) (533), polA (DNA pol I) (30,574), dnaB (replicative DNA helicase) (281), and polC/dnaE (the catalytic subunit of DNA pol III) (282), as well as the unsurprising deficiency of a DNA ligase mutant (755). The filling in of the daughter strand gaps is likely to be carried out by DNA pol I, although in polA mutants the gaps are apparently closed by DNA pol III (with the help of DnaB?…”

Section: One-strand Repair: Lesion Removal and Filling In Of The Gapmentioning

confidence: 99%

Recombinational Repair of DNA Damage in Escherichia coli and Bacteriophage λ

Kuzminov

1999

Microbiol Mol Biol Rev

843

579

View full text Add to dashboard Cite

SUMMARY Although homologous recombination and DNA repair phenomena in bacteria were initially extensively studied without regard to any relationship between the two, it is now appreciated that DNA repair and homologous recombination are related through DNA replication. In Escherichia coli, two-strand DNA damage, generated mostly during replication on a template DNA containing one-strand damage, is repaired by recombination with a homologous intact duplex, usually the sister chromosome. The two major types of two-strand DNA lesions are channeled into two distinct pathways of recombinational repair: daughter-strand gaps are closed by the RecF pathway, while disintegrated replication forks are reestablished by the RecBCD pathway. The phage λ recombination system is simpler in that its major reaction is to link two double-stranded DNA ends by using overlapping homologous sequences. The remarkable progress in understanding the mechanisms of recombinational repair in E. coli over the last decade is due to the in vitro characterization of the activities of individual recombination proteins. Putting our knowledge about recombinational repair in the broader context of DNA replication will guide future experimentation.

show abstract

Expression of the dnaN and dnaQ genes of Escherichia coli is inducible by mitomycin C

Kaasch

Quiñones

1989

Molec. Gen. Genet.

View full text Add to dashboard Cite

The dnaN and dnaQ genes encode the beta subunit and the epsilon subunit of the DNA polymerase III holoenzyme. Using translational fusions to lacZ we found that DNA damage caused by mitomycin C induces expression of the dnaA and dnaQ genes. This induction was not observed in lexA and recA mutants which block the induction of the SOS response, suggesting a relationship between the mechanism(s) of genetic control of DNA polymerase III holoenzyme and the SOS regulatory network. Nevertheless, there is evidence that the mitomycin C induction of dnaN and dnaQ is not a simple lexA-regulated process, because nalidixic acid (an excellent SOS inducer) does not increase dnaN and dnaQ gene expression, and the time course of induction is abnormally slow.

show abstract

Reduction of postreplication DNA repair in two Escherichia coli mutants with temperature-sensitive polymerase III activity: implications for the postreplication repair pathway

Cited by 9 publications

References 7 publications

Replisome activity slowdown after exposure to ultraviolet light in Escherichia coli

Replisome activity slowdown after exposure to ultraviolet light in Escherichia coli

Recombinational Repair of DNA Damage in Escherichia coli and Bacteriophage λ

Expression of the dnaN and dnaQ genes of Escherichia coli is inducible by mitomycin C

Contact Info

Product

Resources

About