A functional map of plasmid ColE1

Dougan, Gordon; Saul, Michael W.; Warren, Gareth J.; Sherratt, David J.

doi:10.1007/bf00267204

Cited by 97 publications

(53 citation statements)

References 17 publications

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“…Plasmid pColE1 was the first plasmid used as a cloning vehicle at the start of the era of genetic engineering in 1974 (263). Its genetic map was first drawn in 1978 (160), and its 6,646 bp were sequenced in 1985 (110). Since then, the complete sequences of pCloDF13 (9,957 bp) and pColA (6,720 bp) have been published (465,480).…”

Section: Introductionmentioning

confidence: 99%

Colicin Biology

Cascales

Buchanan

Duché

et al. 2007

Microbiol Mol Biol Rev

985

1,324

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SUMMARY Colicins are proteins produced by and toxic for some strains of Escherichia coli. They are produced by strains of E. coli carrying a colicinogenic plasmid that bears the genetic determinants for colicin synthesis, immunity, and release. Insights gained into each fundamental aspect of their biology are presented: their synthesis, which is under SOS regulation; their release into the extracellular medium, which involves the colicin lysis protein; and their uptake mechanisms and modes of action. Colicins are organized into three domains, each one involved in a different step of the process of killing sensitive bacteria. The structures of some colicins are known at the atomic level and are discussed. Colicins exert their lethal action by first binding to specific receptors, which are outer membrane proteins used for the entry of specific nutrients. They are then translocated through the outer membrane and transit through the periplasm by either the Tol or the TonB system. The components of each system are known, and their implication in the functioning of the system is described. Colicins then reach their lethal target and act either by forming a voltage-dependent channel into the inner membrane or by using their endonuclease activity on DNA, rRNA, or tRNA. The mechanisms of inhibition by specific and cognate immunity proteins are presented. Finally, the use of colicins as laboratory or biotechnological tools and their mode of evolution are discussed.

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Section: Introductionmentioning

confidence: 99%

Colicin Biology

Cascales

Buchanan

Duché

et al. 2007

Microbiol Mol Biol Rev

985

1,324

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“…Horizontal arrows indicate the direction of transcription of the kanamycin resistance gene. The open box indicates the colicin El gene [ 7 ] ; the slashed box, immunity gene (imm); the black box, the hypothetical gene [lo, 281 and the stippled box; the mobility region [29] coding for the protein. As shown in Fig.4, ColE1 had four AvaII sites, one of which was located within the hypothetical gene [lo, 281.…”

Section: A Gene Located Downstrecinz From the Coliciii E L Gorementioning

confidence: 99%

“…pMY440 and pMY444 were obtained from kanamycinresistant and colicin-E I-producing transformants. In pMY440, the AvaII fragment was inserted in the hypothetical gene, while pMY444 had the insertion in the region required for plasmid mobilization [29].…”

Section: A Gene Located Downstrecinz From the Coliciii E L Gorementioning

confidence: 99%

Factors necessary for the export process of colicin E1 across cytoplasmic membrane of Escherichia coli

Yamada

Nakazawa

1984

Eur J Biochem

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Factors necessary for the export process of colicin E1 across the cytoplasmic membrane of Escherichia coli were investigated. β‐Galactosidase activities from gene fusions between the colicin E1 and lacZ genes were recovered in the inner membrane fraction of E. coli when the region containing the internal signal‐like sequence of colicin E1 [M. Yamada et al. (1982) Proc. Natl Acad. Sci. USA 79, 2827–2831] was present, but were found in the soluble fraction when the region was eliminated. The colicin E1 export was reduced upon insertion mutation in a gene that is located downstream from the colicin E1 gene in the same operon and responsible for mitomycin‐C‐induced killing of the host cell. A frame shift mutation of the colicin E1 plasmid was constructed to direct the protein which had lost the COOH‐terminal 13 residues of original colicin E1 and was altered in 6 residues of the new COOH‐terminal portion. The aberrant colicin E1 that was inducibly synthesized remained inside the cells. These results indicate that colicin E1 is exported with the aid of a product of the downstream gene and that the COOH‐terminal portion is necessary for the export. The binding of colicin E1 to the cytoplasmic membrane through the internal signal‐like sequence may be a step in the protein export process.

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“…It comprises 26-32% of the total pCo1 A. This percentage is almost the same as that occupied in the pCo1 El by the colicin El structural gene (tea), which represents 27% of the total pCo1 El [7]. Both colicins have a similar Mr, 56 000 for Co1 El [8] and 60 000 for Co1 A [3].…”

Section: Localization Of the Co1 A Structural Genementioning

confidence: 99%