Biochemistry of homologous recombination in Escherichia coli.

Kowalczykowski, S. C.; Dixon, D A; Eggleston, Angela K.; Lauder, S D; Rehrauer, W M

doi:10.1128/mmbr.58.3.401-465.1994

Cited by 688 publications

(488 citation statements)

References 428 publications

(807 reference statements)

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“…the plasmid also carries a chi (X) site. The X site is an 8 bp sequence that is recognized by RecBCD enzyme (exonuclease V) and attenuates the nuclease activity of the enzyme (Kowalczykowski et al, 1994). The strains used in the experiment shown in Figure 3 harbored two plasmids, pHKX1-cos and pFMl23.…”

Section: Resultsmentioning

confidence: 99%

Escherichia coli PriA protein is essential for inducible and constitutive stable DNA replication.

et al. 1994

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Under certain conditions, Escherichia coli cells exhibit either of two altered modes of chromosomal DNA replication. These are inducible stable DNA replication (iSDR), seen in SOS‐induced cells, and constitutive stable DNA replication (cSDR), seen in rnhA mutants. Both iSDR and cSDR can continue to occur in the absence of protein synthesis. They are dependent on RecA protein, but do not require DnaA protein or the oriC site. Here we report the requirement for PriA, a protein essential for assembly of the phi X174‐type primosome, for both iSDR and cSDR. In priA1(Null)::kan mutant cells, iSDR is not observed after induction by thymine starvation. Replication from one of the origins (oriM1) specific to iSDR is greatly reduced by the priA1::kan mutation. cSDR in rnhA224 mutant cells deficient in RNase HI is also completely abolished by the same priA mutation. In both cases, SDR is restored by introduction of a plasmid carrying a wild‐type priA gene. Furthermore, the viability of an rnhA::cat dnaA46 strain is lost at 42 degrees C upon inactivation of the priA gene, indicating the lethal effect of priA inactivation on those cells whose viability depends on cSDR. These results demonstrate that a function of PriA protein is essential for iSDR and cSDR and suggest the involvement of the PriA‐dependent phi X174‐type primosome in these DnaA/oriC‐independent pathways of chromosome replication. Whereas ColE1‐type plasmids, known to be independent of DnaA, absolutely require PriA function for replication, DnaA‐dependent plasmid replicons such as pSC101, F, R6K, Rts1 and RK2 are able to transform and to be maintained in the priA1::kan strain.(ABSTRACT TRUNCATED AT 250 WORDS)

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Section: Resultsmentioning

confidence: 99%

Escherichia coli PriA protein is essential for inducible and constitutive stable DNA replication.

et al. 1994

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“…Homologous recombination, in addition to its fundamental role in genetic diversification of bacterial genomes, plays an essential role in the repair of a variety of DNA damage, including double-strand breaks (Kuzminov, 1999;Michel et al, 2004). In Escherichia coli, the initiation of homologous recombination can be carried out by either the RecBCD or the RecFOR proteins; in both cases, these proteins act as mediators for RecA binding to single-stranded DNA (ssDNA) to allow for homologous strand invasion (Kowalczykowski et al, 1994). Comparative studies of bacterial genomes have revealed that many genomes display an incomplete set of DNA repair systems.…”

Section: Introductionmentioning

confidence: 99%

Crystal structure and mutational study of RecOR provide insight into its mode of DNA binding

Timmins

Leiros

McSweeney

2007

EMBO J

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The crystal structure of the complex formed between Deinococcus radiodurans RecR and RecO (drRecOR) has been determined. In accordance with previous biochemical characterisation, the drRecOR complex displays a RecR:RecO molecular ratio of 2:1. The biologically relevant drRecOR entity consists of a heterohexamer in the form of two drRecO molecules positioned on either side of the tetrameric ring of drRecR, with their OB (oligonucleotide/oligosaccharide‐binding) domains pointing towards the interior of the ring. Mutagenesis studies validated the protein–protein interactions observed in the crystal structure and allowed mapping of the residues in the drRecOR complex required for DNA binding. Furthermore, the preferred DNA substrate of drRecOR was identified as being 3′‐overhanging DNA, as encountered at ssDNA–dsDNA junctions. Together these results suggest a possible mechanism for drRecOR recognition of stalled replication forks.

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“…One of the most severe DNA lesions produced by damaging agents are double-stranded breaks (DSBs) that are also induced by disintegration of DNA replication forks. In Bacteria, DSBs are repaired by homologous recombination, whereas, in Eukarya, they are repaired either by homologous or non-homologous recombination (Kowalczykowski et al, 1994;Pâques and Haber, 1999). In Archaea, mechanisms involved in DSB repair have not been clearly identified.…”

Section: Introductionmentioning

confidence: 99%

NurA, a novel 5′–3′ nuclease gene linked to rad50 and mre11 homologs of thermophilic Archaea

2002

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We isolated and characterized a new nuclease (NurA) exhibiting both single-stranded endonuclease activity and 5′-3′ exonuclease activity on single-stranded and double-stranded DNA from the hyperthermophilic archaeon Sulfolobus acidocaldarius. Nuclease homologs are detected in all thermophilic archaea and, in most species, the nurA gene is organized in an operon-like structure with rad50 and mre11 archaeal homologs. This nuclease might thus act in concert with Rad50 and Mre11 proteins in archaeal recombination/repair. To our knowledge, this is the first report of a 5′-3′ nuclease potentially associated with Rad50 and Mre11-like proteins that may lead to the processing of double-stranded breaks in 3′ single-stranded tails.

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Biochemistry of homologous recombination in Escherichia coli.

Abstract: entially affected RecA mutants.421 mutants defective in protein filament formation .421 INZYME (EXONUCLEASE V) .421 al Functions .

Cited by 688 publications

References 428 publications

Escherichia coli PriA protein is essential for inducible and constitutive stable DNA replication.

Escherichia coli PriA protein is essential for inducible and constitutive stable DNA replication.

Crystal structure and mutational study of RecOR provide insight into its mode of DNA binding

NurA, a novel 5′–3′ nuclease gene linked to rad50 and mre11 homologs of thermophilic Archaea

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