Escherichia coli and Bacillus subtilis PriA proteins essential for recombination-dependent DNA replication: Involvement of ATPase/helicase activity of PriA for inducible stable DNA replication

Masai, Hisao; Deneke, Jan; Furui, Yuji; Tanaka, Taku; Arai, Kohei

doi:10.1016/s0300-9084(99)00211-4

Cited by 21 publications

(14 citation statements)

References 39 publications

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“…Furthermore, recombination dependent DNA replication is partially impaired in the ATPase-deficient mutants of PriA (48), validating a helicase requirement. The PriA suppressor mutation, dnaC809, can rescue synthetic lethality between priA and either ftsK, recG, or ruvC (49).…”

Section: Pria and Recombinationmentioning

confidence: 80%

Recruitment to stalled replication forks of the PriA DNA helicase and replisome-loading activities is essential for survival

2010

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PriA, a 3′→5′ superfamily 2 DNA helicase, acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. The ability of PriA to initiate replication at stalled forked structures ensures complete genome replication and helps to protect the cell from illegitimate recombination events. This review focuses on the activities of PriA and its role in replication fork assembly and maintaining genomic integrity.

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Section: Pria and Recombinationmentioning

confidence: 80%

Recruitment to stalled replication forks of the PriA DNA helicase and replisome-loading activities is essential for survival

2010

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“…In the Walker A motif GxxGxGK(T/S), the invariant Lys makes direct contact with the β and γ phosphates of the bound nucleotides, whereas the hydroxyl group of threonine interacts with the β‐phosphates and with magnesium coordinated to the β‐ and γ‐phosphates. We and others have previously reported characterization of the K230D mutant, in which the conserved lysine was mutated to aspartic acid (Zavitz & Marians 1992; Masai et al . 1999).…”

Section: Resultsmentioning

confidence: 99%

“…PriA was shown to bind to synthetic D‐loop or arrested‐fork structures in vitro , and can assemble a similar primosome which supports leading and lagging strand syntheses (McGlynn et al . 1997; Masai et al . 1999; Nurse et al .…”

Section: Introductionmentioning

confidence: 99%

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ATPase/helicase motif mutants of Escherichia coli PriA protein essential for recombination‐dependent DNA replication

et al. 2003

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Backgrounds : PriA protein, a DEXH-type helicase with C 2 C 2 zinc-finger motifs, plays essential roles in RecA-dependent modes of Escherichia coli chromosomal DNA replication, namely inducible and constitutive stable DNA replication (iSDR and cSDR respectively, which may be initiated from a D-loop or R-loop structure), and in repair of doublestranded DNA breaks generated by various genotoxic agents or spontaneously during the course of DNA replication. However, the roles of ATPase/ DNA helicase activities in functions of PriA are not well understood.

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“…When supplied in trans , helicase‐inactive priA alleles with mutations in the Walker box nucleotide binding motif ( priA K230R , priA K230A and priA K230D ) restore apparently wild‐type levels of viability and cell morphology to priA null strains (Zavitz and Marians, 1992; Kogoma et al ., 1996; Sandler et al ., 1996; Masai et al ., 1999). Two of these alleles allow strains to assimilate genetic markers by homologous recombination, albeit at 30–50% of the level of wild type (Zavitz and Marians, 1992; Kogoma et al ., 1996; Sandler et al ., 1996), while the third, priA K230D , supports only low levels of iSDR (Masai et al ., 1999). Work in the Mu system suggests a role for the helicase and also indicates that other proteins in the cell can compensate for the lack of PriA helicase activity (Jones and Nakai, 1999).…”

Section: Fork‐dependent Dna Replication In Escherichia Coli Is Suppormentioning

confidence: 99%

PriA and phage T4 gp59: factors that promote DNA replication on forked DNA substrates

Jones¹,

Nakai²

2000

Molecular Microbiology

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The initiation of DNA synthesis on forked DNA templates is a vital process in the replication and maintenance of cellular chromosomes. Two proteins that promote replisome assembly on DNA forks have so far been identified. In phage T4 development the gene 59 protein (gp59) assembles replisomes at D‐loops, the sites of homologous strand exchange. Bacterial PriA protein plays an analogous function, most probably restarting replication after replication fork arrest with the aid of homologous recombination proteins, and PriA is also required for phage Mu replication by transposition. Gp59 and PriA exhibit similar DNA fork binding activities, but PriA also has a 3′ to 5′ helicase activity that can promote duplex opening for replisome assembly. The helicase activity allows PriA’s repertoire of templates to be more diverse than that of gp59. It may give PriA the versatility to restart DNA replication without recombination on arrested replication forks that lack appropriate duplex openings.

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Escherichia coli and Bacillus subtilis PriA proteins essential for recombination-dependent DNA replication: Involvement of ATPase/helicase activity of PriA for inducible stable DNA replication

Cited by 21 publications

References 39 publications

Recruitment to stalled replication forks of the PriA DNA helicase and replisome-loading activities is essential for survival

Recruitment to stalled replication forks of the PriA DNA helicase and replisome-loading activities is essential for survival

ATPase/helicase motif mutants of Escherichia coli PriA protein essential for recombination‐dependent DNA replication

PriA and phage T4 gp59: factors that promote DNA replication on forked DNA substrates

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