Antirestriction and antimodification activities of T7 Ocr: Effects of amino acid substitutions in the interface

Zavilgelsky, G. B.; Kotova, V. Yu.; Расторгуев, С. М.

doi:10.1134/s0026893309010130

Cited by 11 publications

(12 citation statements)

References 16 publications

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“…Ocr is a striking example of DNA mimicry by a protein. It is a homodimer of two 116-aa subunits ( 127 ) that interface by a complementary fit of hydrophobic surfaces [( 141 , 158 ); pdb:1S7Z and 2Y7C; Figure 3 ]. The dimer is banana shaped with a length of ∼7.5 nm and a general width of 2 nm thickening to 2.5 nm at the dimer interface ( 141 , 159 , 160 ).…”

Section: Control Of R–m Activitymentioning

confidence: 99%

“…The effectiveness of Ocr, ArdA and ArdB in inhibiting restriction and modification by Type I enzymes has usually been investigated in vivo by comparing the eop of phage on restriction-proficient hosts with or without antiR–M genes ( 139 , 141 , 142 , 145 , 158 , 167 ). Active antiR enhances the number of recovered phage, and these in turn can then be tested for modification by their eop on restriction-proficient and -deficient strains.…”

Section: Control Of R–m Activitymentioning

confidence: 99%

“…Active antiR enhances the number of recovered phage, and these in turn can then be tested for modification by their eop on restriction-proficient and -deficient strains. Quantitative comparisons in these experiments are difficult due to varying experimental details, but the in vivo titration assay, in which an inducible promoter and antiR–M expression is controlled by inducer concentration, recently introduced by the group of Zavil’gel’skii, suggests a good way forward for quantitative comparison of antiR–M systems ( 139 , 158 , 167 ).…”

Section: Control Of R–m Activitymentioning

confidence: 99%

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Type I restriction enzymes and their relatives

Loenen

Dryden

Raleigh

et al. 2013

Nucleic Acids Research

219

245

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Type I restriction enzymes (REases) are large pentameric proteins with separate restriction (R), methylation (M) and DNA sequence-recognition (S) subunits. They were the first REases to be discovered and purified, but unlike the enormously useful Type II REases, they have yet to find a place in the enzymatic toolbox of molecular biologists. Type I enzymes have been difficult to characterize, but this is changing as genome analysis reveals their genes, and methylome analysis reveals their recognition sequences. Several Type I REases have been studied in detail and what has been learned about them invites greater attention. In this article, we discuss aspects of the biochemistry, biology and regulation of Type I REases, and of the mechanisms that bacteriophages and plasmids have evolved to evade them. Type I REases have a remarkable ability to change sequence specificity by domain shuffling and rearrangements. We summarize the classic experiments and observations that led to this discovery, and we discuss how this ability depends on the modular organizations of the enzymes and of their S subunits. Finally, we describe examples of Type II restriction–modification systems that have features in common with Type I enzymes, with emphasis on the varied Type IIG enzymes.

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Section: Control Of R–m Activitymentioning

confidence: 99%

Section: Control Of R–m Activitymentioning

confidence: 99%

Section: Control Of R–m Activitymentioning

confidence: 99%

See 1 more Smart Citation

Type I restriction enzymes and their relatives

Loenen

Dryden

Raleigh

et al. 2013

Nucleic Acids Research

219

245

View full text Add to dashboard Cite

show abstract

“…To estimate the intracellular concentration of anti restriction proteins, we employed a bioluminescence method, which was developed earlier and utilized pZE21 lux as a biosensor plasmid [14].…”

Section: Construction Of Hybrid Plasmidsmentioning

confidence: 99%

Comparative analysis of antirestriction activity of the ArdA and ArdB proteins encoded by genes of the R64 transmissible plasmid (IncI1)

2012

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Antirestriction proteins ArdA and ArdB are specific inhibitors of type I restriction-modification enzymes. The ardA and yfeB (ardB) genes were cloned from the transmissible plasmid R64 in the pUC18 and pZE21 vectors. The R64 ArdA and ArdB proteins were shown to inhibit only restriction activity of the type I restriction-modification enzyme (EcoKI) in Escherichia coli K12 cells. In contrast to ArdA, ArdB inhibited EcoKI restriction activity only at a high intracellular concentration. Antirestriction activity of ArdB did not depend on the ClpXP protease. The yfeB (ardB) gene of the R64 plasmid is transcribed from a weak promoter located upstream of yfeA.

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“…In addition, the mutant protein Ocr F53D A57E has a K d of 10 -7 M, which is 1000 times higher than the K d of the native Ocr form (Fig. 6) (Zavilgelsky et al, 2009 Notes: * Phage λ.0 was used to infect E. coli JM109 r-m+ cells. A phage lysate obtained after one reproduction cycle (λjm109) was titrated on strains TG_1 and AB1157.…”

Section: Anhydrotetracyclinmentioning

confidence: 99%