Colicin Import into<i>Escherichia coli</i>Cells

Lazdunski, Claude; Bouveret, Emmanuelle; Rigal, Alain; Journet, Laure; Lloubès, Roland; Bénédetti, Hélène

doi:10.1128/jb.180.19.4993-5002.1998

Cited by 168 publications

(116 citation statements)

References 124 publications

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“…This is consistent with the observation that expression of the orf1tolQRA operon is also regulated by RcsC, the cytoplasmic membrane sensor protein of the RcsB-RcsC two-component system involved in the regulation of capsule synthesis [12]. The TolQRA proteins are required for the translocation of the ¢lamentous bacteriophage DNA into the cytoplasm during the process of infection [13,14], and also participate in the translocation of group A colicins to their respective sites of action [15].…”

Section: The Tol Proteinssupporting

confidence: 87%

The Tol proteins of Escherichia coli and their involvement in the uptake of biomolecules and outer membrane stability

Lazzaroni

1999

FEMS Microbiology Letters

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The Tol proteins of Escherichia coli are involved in outer membrane stability. They are also required for the uptake of the group A colicins and the translocation of filamentous phage DNA into the cytoplasm. The tol-pal genes constitute two operons in the E. coli genome, orf1tolQRA and tolBpalorf2. The TolQ TolR TolA proteins form a complex in the cytoplasmic membrane, while TolB and Pal interact near the outer membrane. Most of the amino acid residues of TolA, TolB, TolR and Pal are localized in the periplasm. Recent advances in the knowledge of interactions of Tol-Pal proteins with other envelope components, or with group A colicins, are presented, together with current hypotheses about the role of the Tol proteins in outer membrane stability. ß

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Section: The Tol Proteinssupporting

confidence: 87%

The Tol proteins of Escherichia coli and their involvement in the uptake of biomolecules and outer membrane stability

Lazzaroni

1999

FEMS Microbiology Letters

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“…It has been estimated that just one colicin molecule is required to kill a bacterial cell (Nomura, 1967). Colicins fall into two groups: group A colicins are translocated across the outer membrane with the help of the Tol system, consisting of proteins TolA, TolB, TolQ, TolR, and Pal (Lazdunski et al, 1998). Group B colicins require the Ton system, consisting of proteins TonB, ExbB, and ExbD (Braun et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

Structure of colicin I receptor bound to the R-domain of colicin Ia: implications for protein import

Buchanan

Lukacik

Grizot

et al. 2007

EMBO J

107

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Colicin Ia is a 69 kDa protein that kills susceptible Escherichia coli cells by binding to a specific receptor in the outer membrane, colicin I receptor (70 kDa), and subsequently translocating its channel forming domain across the periplasmic space, where it inserts into the inner membrane and forms a voltage-dependent ion channel. We determined crystal structures of colicin I receptor alone and in complex with the receptor binding domain of colicin Ia. The receptor undergoes large and unusual conformational changes upon colicin binding, opening at the cell surface and positioning the receptor binding domain of colicin Ia directly above it. We modelled the interaction with full-length colicin Ia to show that the channel forming domain is initially positioned 150 Å above the cell surface. Functional data using full-length colicin Ia show that colicin I receptor is necessary for cell surface binding, and suggest that the receptor participates in translocation of colicin Ia across the outer membrane.

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“…The ExbB, ExbD and TonB proteins exhibit significant similarities to the TolQ, TolR and TolA proteins, respectively (Lazdunski et al, 1998), and a common evolutionary origin between TolA domain III and the C-terminal domain of TonB has been proposed (Witty et al, 2002). Mutations in the tol system of Gram-negative bacteria lead to debilitated membranes and to the release of periplasmic proteins to the outer medium (Fognini-Lefebvre et al, 1987;Llamas et al, 2000).…”

Section: Kbmentioning

confidence: 99%

Pseudomonas putida mutants in the exbBexbDtonB gene cluster are hypersensitive to environmental and chemical stressors

Godoy

Ramos-González

Ramos

2004

Environmental Microbiology

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The genes in the exbBexbDtonB cluster of Pseudomonas putida DOT-T1E are co-transcribed. We have generated non-polar mutants in each of the genes by inserting an aphA3 cassette encoding kanamycin resistance. All three mutants show similar phenotypes: the mutants are unable to grow on minimal medium under iron deficiency conditions. Furthermore, regardless of iron conditions, all mutants are hypersensitive to antibiotics, p-hydroxybenzoate and toluene, chemicals that are extruded from the cell by efflux pumps. These findings are discussed in terms of the involvement of the TonB system in the energization of outer membrane functions necessary for the import or export of different compounds in P. putida.

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Colicin Import intoEscherichia coliCells

Cited by 168 publications

References 124 publications

The Tol proteins of Escherichia coli and their involvement in the uptake of biomolecules and outer membrane stability

The Tol proteins of Escherichia coli and their involvement in the uptake of biomolecules and outer membrane stability

Structure of colicin I receptor bound to the R-domain of colicin Ia: implications for protein import

Pseudomonas putida mutants in the exbBexbDtonB gene cluster are hypersensitive to environmental and chemical stressors

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