Genetic Location of Certain Mutations Conferring Recombination Deficiency in
            <i>Escherichia coli</i>

Willetts, Neil; Clark, Alvin J.; Low, Brooks

doi:10.1128/jb.97.1.244-249.1969

Cited by 347 publications

(131 citation statements)

References 5 publications

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“…All bacterial strains used in this work are derivatives of E. coli K-12 and are described in Table 1. The protocol for P1 transduction has been described elsewhere (Willetts et al, 1969). All P1 transductions were selected on 2% agar plates containing either minimal or rich media.…”

Section: Bacterial Strainsmentioning

confidence: 99%

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Measurement of SOS expression in individual Escherichia coli K‐12 cells using fluorescence microscopy

McCool

Long

Petrosino

et al. 2004

Molecular Microbiology

164

185

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SummaryMany recombination, DNA repair and DNA replication mutants have high basal levels of SOS expression as determined by a sulAp-lacZ reporter gene system on a population of cells. Two opposing models to explain how the SOS expression is distributed in these cells are: (i) the 'Uniform Expression Model (UEM)' where expression is evenly distributed in all cells or (ii) the 'Two Population Model (TPM)' where some cells are highly induced while others are not at all. To distinguish between these two models, a method to quantify SOS expression in individual bacterial cells was developed by fusing an SOS promoter ( sulAp ) to the green fluorescent protein ( gfp ) reporter gene and inserting it at att l l l l on the Escherichia coli chromosome. It is shown that the fluorescence in sulAp-gfp cells is regulated by RecA and LexA. This system was then used to distinguish between the two models for several mutants. The patterns displayed by priA , dnaT , recG , uvrD , dam , ftsK , rnhA , polA and xerC mutants were explained best by the TPM while only lexA (def) , lexA3 (ind -) and recA defective mutants were explained best by the UEM. These results are discussed in a context of how the processes of DNA replication and recombination may affect cells in a population differentially.

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Section: Bacterial Strainsmentioning

confidence: 99%

“…Cultures were grown in 56/2 minimal medium (Willetts et al, 1969) until mid-log phase (OD 600 = 0.3-0.4). Cells were concentrated 10-fold in 56/2 buffer and mixed with an equal volume of reference beads (In-Speck, Molecular Probes).…”

Section: Preparation Of Bacteria For Microscopymentioning

confidence: 99%

Measurement of SOS expression in individual Escherichia coli K‐12 cells using fluorescence microscopy

McCool

Long

Petrosino

et al. 2004

Molecular Microbiology

164

185

View full text Add to dashboard Cite

show abstract

“…All bacterial strains used in this work are derivatives of E. coli K-12 and are described in Table 1. The protocol for P1 transduction has been described elsewhere (Willetts et al, 1969). All strains were grown in 56/2 minimal media (Willetts et al, 1969).…”

Section: Bacterial Strains and Plasmidsmentioning

confidence: 99%

PriA mutations that affect PriA–PriC function during replication restart

Sandler¹,

McCool

Thien

et al. 2001

Molecular Microbiology

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In Escherichia coli, repair and restart of collapsed replication forks is thought to be essential for cell growth. The replication restart proteins, PriA, PriB, PriC, DnaB, DnaC, DnaG, DnaT and Rep, form redundant pathways that recognize repaired replication forks and restart them. Recognition, modulation of specific DNA structures and loading of the replicative helicase by the replication restart proteins, is likely to be important for replication restart. It has been hypothesized that PriB and PriC function with PriA in genetically separate and redundant PriA–PriB and PriA–PriC pathways. In this study, the del(priB)302 or priC303::kan mutations were used to isolate the PriA–PriB and PriA–PriC pathways genetically so that the effects of three priA missense mutations, priA300 (K230R), priA301 (C479Y) and priA306 (L557P), on these pathways could be assessed. In a wild‐type background, the three priA mutations had little, if any, effect on the phenotypes of UV resistance, basal levels of SOS expression and cell viability. In the priB mutant, priA300 and priA301 caused dramatic negative changes in the three phenotypes listed above (and others), whereas the third priA mutant allele, priA306, showed very little negative effect. In the priC mutant, all three priA mutations behaved similarly, producing little, if any, changes in phenotypes. We conclude that priA300 and priA301 mostly affect the PriA–PriC pathway and do so more than priA306. We suggest that PriA's helicase activity is important for the PriA–PriC pathway of replication restart.

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“…Phage transduction P1 transducing lysates were prepared as described by Buxton and Holland (1973) and transductions carried out as described by Willetts et al (1969). Where necessary, recipients were grown in nutrient broth for 2 h to allow expression of specific markers before plating onto selective media.…”

Section: Strainsmentioning

confidence: 99%

Inactivation of essential division genes, ftsA, ftsZ, suppresses mutations at sfiB, a locus mediating division inhibition during the SOS response in E. coli.

Jones¹,

Holland²

1984

The EMBO Journal

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A dominant sfiB allele has been cloned which renders partial diploids of an sfiB + Escherichia coli host resistant to division inhibition mediated by the SOS response. Transpositional mutagenesis was used to map the position of this sfiB114 allele, carried by a plasmid pLG552, to an approximately 0.6‐kb region overlapping the coding regions for ftsA and ftsZ, two genes essential for normal division. Most Tn 1000 insertions which inactivated sfiB114 also inactivated the ftsA function and caused the disappearance of both a 47‐K polypeptide and reduced levels of a 42‐K polypeptide in maxi‐cells carrying pLG552 . An additional insertion inactivating sfiB114 was mapped to the right of ftsA and resulted in loss of the 42‐K but not the 47‐K polypeptide in maxi‐cells. Moreover, a 2.1‐kb BamHI‐EcoRI DNA fragment was subcloned which carried ftsA and coded for a 47‐K polypeptide but did not carry sfiB114 and did not complement ftsZ . We conclude that sfiB114 is located within ftsZ coding for a 42‐K polypeptide. Nevertheless, insertions into ftsZ coding the 47‐K polypeptide suppress the sfiB114 allele by substantially reducing the synthesis of the FtsZ (SfiB114) polypeptide. The level of residual FtsZ synthesis was minimal when Tn 1000 was inserted closest to the distal end of ftsA, indicating the presence of a regulatory region essential for maximal expression of ftsZ .

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Genetic Location of Certain Mutations Conferring Recombination Deficiency in Escherichia coli

Cited by 347 publications

References 5 publications

Measurement of SOS expression in individual Escherichia coli K‐12 cells using fluorescence microscopy

Measurement of SOS expression in individual Escherichia coli K‐12 cells using fluorescence microscopy

PriA mutations that affect PriA–PriC function during replication restart

Inactivation of essential division genes, ftsA, ftsZ, suppresses mutations at sfiB, a locus mediating division inhibition during the SOS response in E. coli.

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