Regulation of the BamHI restriction-modification system by a small intergenic open reading frame, bamHIC, in both Escherichia coli and Bacillus subtilis

Ives, Catherine L.; Nathan, Peter D.; Brooks, Joan E.

doi:10.1128/jb.174.22.7194-7201.1992

Cited by 65 publications

(45 citation statements)

References 41 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…2). Similar experiments had previously established a restriction activator role for CؒPvuII (Tao et al, 1991) and CؒBamHI (Ives et al, 1992) in the in vivo expression of their cognate restriction enzymes. Therefore, the overall effect of CؒLlaI was similar to the proposed role for the type II enzyme C protein family.…”

Section: Discussionmentioning

confidence: 77%

“…The second controller protein investigated was for the BamHI R/M system from Bacillus amyloliquefaciens. A similar role for CؒBamHI as a positive regulator of transcription of bamHIR was found, but in addition the controller protein was also proposed to act as a negative regulator of bamHIM (Ives et al, 1992). No direct evidence for transcription regulation by any C protein has been presented to date, but the cumulative data suggest this is the most likely mechanism (Ives et al, 1995).…”

Section: Introductionmentioning

confidence: 92%

See 1 more Smart Citation

Control of expression of LlaI restriction in Lactococcus lactis

O’Sullivan

Klaenhammer

1998

Molecular Microbiology

View full text Add to dashboard Cite

SummaryThe plasmid encoded LlaI R/M system from Lactococcus lactis ssp. lactis consists of a bidomain methylase, with close evolutionary ties to type IIS methylases, and a trisubunit restriction complex. Both the methylase and restriction subunits are encoded on a polycistronic 6.9 kb operon. In this study, the 5Ј end of the llaI 6.9 kb transcript was determined by primer extension analysis to be 254 completely abolished any enhancement of restriction activity. These data provide molecular evidence for a mechanism on how the expression of a restriction system in a prokaryote can be drastically reduced during elevated growth temperatures, by a small regulatory protein.

show abstract

Section: Discussionmentioning

confidence: 77%

Section: Introductionmentioning

confidence: 92%

Control of expression of LlaI restriction in Lactococcus lactis

O’Sullivan

Klaenhammer

1998

Molecular Microbiology

View full text Add to dashboard Cite

show abstract

“…Other restriction-modification systems have been demonstrated to be controlled (14,22). In cases for which such control has been described, it has been due to the presence of a small open reading frame in the cloned restrictionmodification system that has trans-regulatory properties.…”

Section: Discussionmentioning

confidence: 99%

Induction of EcoRII methyltransferase: evidence for autogenous control

Friedman

Som

1993

J Bacteriol

View full text Add to dashboard Cite

The cytosine analog 5-azacytidine kills Escherichia coli cells that carry plasmids expressing EcoRII DNA (cytosine 5)methyltransferase under control of its own promoter. We previously showed that this enzyme binds tightly to azacytidine-containing DNA in vitro and proposed that such binding is lethal in vivo. In support of this proposal, we now show that the enzyme sediments with the nucleoid of azacytidine-treated cells. Azacytidine treatment led to an increase in the amount of enzyme, and this increase required sequences in the ecoRIIM promoter region. Enzyme inducibility correlated with drug sensitivity: plasmids carrying the methyltransferase gene but lacking the wild-type promoter did not confer sensitivity. These results suggested that the ecoRIIM gene was under autogenous control. Transcriptional ecoRJIM'-lacZ fusions in E. coli were, therefore, constructed. They showed that expression from the ecoRIIM promoter was inhibited when EcoRU DNA (cytosine-5)methyltransferase was introduced into the cell in trans and inhibition was reversed by treating the cells with azacytidine. These results provide evidence that the expression of the ecoRIIM gene is under autogenous regulation and that cell death induced by azacytidine is due, in part, to the disruption of autoregulation.5-Azacytidine (azaCyd) is a nucleoside analog that selectively kills Escherichia coli when the bacteria carry plasmids that specify the EcoRII restriction-modification system (7). The killing is dependent on the presence of the methyltransferase (MTase) and not the restriction enzyme. This phenomenon was also demonstrated when other MTases were cloned and expressed in E. coli on multicopy plasmids (2, 16). The effect appeared to be dependent on the amount of MTase present in the cell (7). With the endogenous Dcm MTase there was little effect of the drug. When this MTase was cloned onto a multicopy plasmid and introduced into E. coli, the strain became sensitive to azaCyd (2). A similar but less dramatic effect was also noted when the MspI MTase, cloned in pBR322, was introduced into E. coli (16).Cells deficient in any of a number of different repair enzymes have enhanced sensitivity to azaCyd. These results imply that the drug causes DNA damage. Support for this conclusion includes the observations that the drug is a weak inducer of the SOS system and is a mutagen in E. coli (1, 16). Although the drug is known to undergo ring opening under mild conditions, it has not been shown that DNA strand breaks occur in vivo.We have shown that the drug inhibits DNA (cytosine-5)methyltransferases (5, 6) once the drug is incorporated into DNA in the sequence CC(A/T)GG (9). We proposed that the basis for cell death was the binding of the enzyme to azacytosine-containing DNA (azaC-DNA), which would inhibit the ability of the cell to repair DNA damage caused by azaCyd (13). In support of this suggestion, we demonstrated that DNA containing azaCyd will not undergo recA-mediated strand exchange if the EcoRII DNA (cytosine-5)methyltransferase (M.EcoRII) is boun...

show abstract

“…These helix-turn-helix proteins have been shown to act as regulators of both their own transcription and that of the restriction endonuclease (ENase) encoded within the same operon. In some cases, C proteins also regulate transcription of the methyltransferase (MTase; Tao et al, 1991;Ives et al, 1992;Rimšelienė et al, 1995;Lubys et al, 1999;Č esnavičienė et al, 2003;Semenova et al, 2005;Bogdanova et al, 2008).…”

Section: Introductionmentioning

confidence: 99%

Overexpression, purification and preliminary X-ray diffraction analysis of the controller protein C.Csp231I fromCitrobactersp. RFL231

2009

View full text Add to dashboard Cite

Restriction-modification controller proteins play an essential role in regulating the temporal expression of restriction-modification genes. The controller protein C.Csp231I represents a new class of controller proteins. The gene was sublconed to allow overexpression in Escherichia coli. The protein was purified to homogeneity and crystallized using the hanging-drop vapour-diffusion method. The crystals diffracted to 2.0 Å resolution and belonged to space group P2 1. An electrophoretic mobility-shift assay provided evidence of strong binding of C.Csp231I to a sequence located upstream of the csp231IC start codon. crystallization communications Acta Cryst. (2009). F65, 898-901 Streeter et al. C.Csp231i 901 Figure 5 Self-rotation function showing NCS. The self-rotation function is shown using a angle of 180 and was calculated using data in the resolution range 20.0-4.0 Å. The radius of integration was 35 Å .

show abstract

Regulation of the BamHI restriction-modification system by a small intergenic open reading frame, bamHIC, in both Escherichia coli and Bacillus subtilis

Cited by 65 publications

References 41 publications

Control of expression of LlaI restriction in Lactococcus lactis

Control of expression of LlaI restriction in Lactococcus lactis

Induction of EcoRII methyltransferase: evidence for autogenous control

Overexpression, purification and preliminary X-ray diffraction analysis of the controller protein C.Csp231I fromCitrobactersp. RFL231

Contact Info

Product

Resources

About