A bacteriocinogenic factor of Enterobacter cloacae

Tieze, G. A.; Stouthamer, A. H.; Jansz, H.S.; Zandberg, J.; Bruggen, E.F.J. Van

doi:10.1007/bf00332820

Cited by 56 publications

(31 citation statements)

References 38 publications

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“…These plasmids include pI5A (5), RSF1030 (6), and CloDF13 (7). As shown here, each of these plasmids specifies transcripts which are analogous to the two ColE 1 transcripts in both size and function.…”

mentioning

confidence: 97%

Inhibition of ColE1 RNA primer formation by a plasmid-specified small RNA.

Tomizawa¹,

Itoh²,

Selzer³

et al. 1981

Proc. Natl. Acad. Sci. U.S.A.

311

150

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Transcription of ColEl DNA by RNA polymerase in vitro starts at two sites in a region required for maintenance of the plasmid. Certain transcripts that start at one of the sites can be cleaved by RNase H and then act as primers for DNA replication. Transcription from the other site produces a RNA -108 nucleotides long (species I or RNA I). Transcripts analogous to the primer and RNA I of ColEl are produced when pl5A or small derivatives of two other ColE1-compatible plasmids, CloDF13 and RSF1030, are used as template. If purified RNA I is added to the transcription reaction containing RNase H, formation of primer is inhibited. Each RNA I can inhibit primer formation by the plasmid that specifies it but has no effect on primer formation by heterologous templates. Thus, the inhibition of primer formation by RNA I is incompatibility specific. Because RNA I does not inhibit initiation or propagation of transcription or the processing of preformed precursors, the step that is sensitive to inhibition is probably formation of the hybrid between the primer precursor and the template. This hybrid is the required substrate for RNase H. Experiments with recombinant plasmids show the region that determines the specificity of response to RNA I to be >300 base pairs upstream of the origin of DNA replication.

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mentioning

confidence: 97%

Inhibition of ColE1 RNA primer formation by a plasmid-specified small RNA.

Tomizawa¹,

Itoh²,

Selzer³

et al. 1981

Proc. Natl. Acad. Sci. U.S.A.

311

150

View full text Add to dashboard Cite

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“…In this latter host the plasmid is present to the extent of about 10 copies per cell (27). A small DNA region located between 1.8 and 11.5% of the CloDF13 genome is essential for autonomous replication (25,31).…”

mentioning

confidence: 99%

Methylation-dependent transcription controls plasmid replication of the CloDF13 cop-1(Ts) mutant

Putten¹,

Lang²,

Veltkamp³

et al. 1986

J Bacteriol

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The CloDF13 cop-l(Ts) mutant expresses a temperature-dependent plasmid copy number. At 42°C the mutant shows a "runaway" behavior, and cells harboring this plasmid are killed. The cop-l(Ts) mutation is a G-to-A transition that disturbs one of the two methylation sites which are located opposite in the stem-loop structure within a region involved in both the initiation of primer synthesis for DNA replication and the termination of the cloacin operon transcript. We demonstrate that the mutation results in an increased primer (RNA II) synthesis resulting from nonconditional enhanced RNA II promoter activity, which at 42°C causes a decrease in the amount of active replication repressor molecules (RNA I) synthesized from the opposite strand. We found that the absence of Dam methylation abolishes the mutant phenotype and that under this condition the high mutant level of RNA H synthesis is reduced, which is accompanied by a restoration of the regulation by RNA I. The role of methylation in the regulation of plasmid replication is discussed.

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“…The cloacinogenic plasmid DF13 (Clo DF13) originates from Enterobacter cloacae; however, Escherichia coli can serve as host as well, since biologically active Clo DF13-specific deoxyribonucleic acid, ribonucleic acid, and proteins are synthesized in E. coli (12,25,26). The Clo DF13 plasmid directs the synthesis of an antibiotic protein, cloacin DF13, which inhibits the protein synthesis in sensitive strains by causing cleavage of a small fragment from the 3' end of the 16S ribonucleic acid of the 30S ribosomal subunit.…”

mentioning

confidence: 99%

Bacteriocinogenic Clo DF13 Minicells of Escherichia coli Synthesize a Protein That Accounts for Immunity to Bacteriocin Clo DF13: Purification and Characterization of the Immunity Protein

Kool

Pols

Nijkamp

1975

Antimicrob Agents Chemother

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Cloacin DF13 inhibits protein synthesis both in vivo and in vitro by inactivation of ribosomes. In this paper we describe the purification, from purified bacteriocinogenic plasmid DF13 (Clo DF13)-harboring minicells of Escherichia coli , of an acidic protein (molecular weight about 10,000) that prevents the inhibition of in vitro protein synthesis by cloacin DF13. It turned out that this protein is one of three Clo DF13 plasmid-specific polypeptides that are synthesized by the noninduced Clo DF13 plasmid in minicells. Furthermore, we observed that, after induction with mitomycin C, the amount of immunity protein is only slightly increased, whereas the cloacin DF13 synthesis is increased about 40 times. These results imply that the genes that code for immunity protein and cloacin DF13 are not located in the same regulatory unit. Under noninduced conditions, apparently an excess of immunity protein is synthesized, because this amount of immunity protein is even sufficient to neutralize the strongly increased amount of cloacin after induction, since growth of induced cloacinogenic cells is continued.

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A bacteriocinogenic factor of Enterobacter cloacae

Cited by 56 publications

References 38 publications

Inhibition of ColE1 RNA primer formation by a plasmid-specified small RNA.

Inhibition of ColE1 RNA primer formation by a plasmid-specified small RNA.

Methylation-dependent transcription controls plasmid replication of the CloDF13 cop-1(Ts) mutant

Bacteriocinogenic Clo DF13 Minicells of Escherichia coli Synthesize a Protein That Accounts for Immunity to Bacteriocin Clo DF13: Purification and Characterization of the Immunity Protein

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