Role of murein lipoprotein in morphogenesis of the bacterial division septum: phenotypic similarity of lkyD and lpo mutants

Fung, J C; MacAlister, T J; Rothfield, Lawrence

doi:10.1128/jb.133.3.1467-1471.1978

Cited by 68 publications

(40 citation statements)

References 6 publications

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“…The poles, however, are ‘free’ of peptidoglycan and can present a point of cell weakness. It is also known that ingrowth of the outer membrane can be dissociated from ingrowth of the division septum by mutations, and that this affects the attachment of the murein layer to the outer membrane, which in turn favours plasmolysis (Rothfield and Justice, 1997; Fung et al ., 1978). Our EM studies have revealed that solvent exposure in the CyoB mutant induces plasmolysis from one of the poles.…”

Section: Discussionmentioning

confidence: 99%

Plasmolysis induced by toluene in a cyoB mutant of Pseudomonas putida

Duque

García

Torre

et al. 2004

Environmental Microbiology

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The cyoABCDE gene cluster of Pseudomonas putida DOT-T1E encodes a terminal cytochrome oxidase. A 500-bp 'cyoB' DNA fragment was cloned in pCHESI Omega Km and used to generate a cyoB knock-out mutant in vivo. The mutant strain was not limited in the generation of proton-motif force, although when grown on minimal medium with glucose or citrate, the CyoB mutant exhibited a slight increase in duplication time with respect to the wild-type strain. This effect was even more pronounced when toluene was supplied in the gas phase. In consonance with the negative effect of toluene on the growth was the finding that the CyoB mutant was hypersensitive to sudden 0.3% (v/v) toluene shocks, in contrast with the wild-type strain. This effect was particularly exacerbated in cells that reached the stationary phase. The increased sensitivity to solvents of the CyoB mutant did not appear to be related to the inability of the cells to strengthen the membrane package or to induce the efflux pumps in response to the solvent, but rather to solvent-induced plasmolysis that may be triggered by wrinkles in the cytoplasmic membrane at the poles of the mutant cells, and invagination of the outer membranes, which eventually lead to cell death.

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Section: Discussionmentioning

confidence: 99%

Plasmolysis induced by toluene in a cyoB mutant of Pseudomonas putida

Duque

García

Torre

et al. 2004

Environmental Microbiology

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“…Another alternative would be that Tol-Pal is involved in a structural protein network that ensures the stability of the outer membrane. In fact, tol-pal mutants share many phenotypes with lpp mutants lacking the major outer membrane lipoprotein: release of periplasmic content, hypersensitivity to various antibacterial agents and loss of outer membrane integrity causing blebbings of the outer membrane in the tol-pal mutants and its invagination at the level of the division septum in lpp mutants (Fung et al, 1978). Therefore, like Lpp and, to a lesser extent, OmpA, the Pal and Tol proteins might be necessary to maintain a functional link between the outer membrane and the peptidoglycan.…”

Section: Introductionmentioning

confidence: 99%

TolB protein ofEscherichia coliK‐12 interacts with the outer membrane peptidoglycan‐associated proteins Pal, Lpp and OmpA

Clavel

Germon

Vianney

et al. 1998

Molecular Microbiology

134

170

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SummaryThe Tol-Pal proteins of Escherichia coli are involved in maintaining outer membrane integrity. Transmembrane domains of TolQ, TolR and TolA interact in the cytoplasmic membrane, while TolB and Pal form a complex near the outer membrane. TolB and the central domain of TolA interact in vitro with the outer membrane porins. In this study, both genetic and biochemical analyses were carried out to analyse the links between TolB, Pal and other components of the cell envelope. It was shown that TolB could be cross-linked in vivo with Pal, OmpA and Lpp, while Pal was associated with TolB and OmpA. The isolation of pal and tolB mutants disrupting some interactions between these proteins represents a first approach to characterizing the residues contributing to the interactions. We propose that TolB and Pal are part of a multiprotein complex that links the peptidoglycan to the outer membrane. The Tol-Pal proteins might form transenvelope complexes that bring the two membranes into close proximity and help some outer membrane components to reach their final destination.

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“…Sensitivity to toxic agents. Pleiotropic envelope-defective mutants of E. coli and S. typhimurium which secrete periplasmic proteins (7,17,32) have been reported to show altered sensitivities to agents such as EDTA, antibiotics, and detergents. We compared strain AE84064 Iky::Mucts with its parent, AE84 Iky+, for growth inhibition by the agents listed in Table 3.…”

Section: Resulttsmentioning

confidence: 99%

“…The loss of the major outer membrane protein, the murein lipoprotein, has been reported to result in detergent and antibiotic sensitivity, as well as the periplasmic leaky phenotype (7,11). To test whether the constellation of envelope leakiness and detergent sensitivity, per se, also conferred colicin resistance, we compared a strain, JE5505 carrying a deletion for the lipoprotein (ipo; 11), with its parent, strain JE5506, lpo+ for resistance to colicn El, by the dilution endpoint method.…”

Section: Resulttsmentioning

confidence: 99%

“…Previously described examples are the lipopolysaccharide (LPS)-defective "deep rough" mutants of Salmonella typhimurium (17) and the lipoprotein-defective strains of E. coli (13,31) and S. typhimurium (7). During the routine screening of phage Mucts-induced mutants of E. coli K-12 defective in leucine transport (1), we discovered a class of "leaky" mutants which secreted periplasmic components, including the leucine-binding proteins, in large amounts.…”

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confidence: 99%

See 1 more Smart Citation

Defective transport and other phenotypes of a periplasmic "leaky" mutant of Escherichia coli K-12

Anderson¹,

Wilson²,

Oxender³

1979

J Bacteriol

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A mutant of Escherichia coli K-12 deficient in high-affinity leucine transport and related binding proteins was obtained by selecting for azaleucine resistance after bacteriophage Mu mutagenesis. We determined that the cause was a generalized loss of periplasmic binding proteins and a sharp decrease in the activity of transport systems requiring them. Other transport systems resistant to osmotic shock and present in membrane vesicles, were affected to a lesser degree or not at all. The mutation, designated lky::Mucts, was shown to be a pleiotropic envelope mutation, rendering the mutant sensitive to ionic and nonionic detergents, antibiotics, and ethylenediaminetetraacetic acid: the strain had also acquired tolerance to colicins E1, E2, and E3, while remaining normally sensitive to a variety of bacteriophages. An analysis of the lipopolysaccharide of parent and mutant strains revealed a twofold reduction in the neutral sugar content of the core oligosaccharide of the lky strain, but no change in sensitivities to phages which utilize lipopolysaccharide or outer membrane proteins for absorption. The lky::Mucts locus was mapped by transduction and found to be located near, or in, the tolPAB gene cluster linked to gal. Secondary mutations suppressing the detergent sensitivity of lky arose at a frequency of 10(-7), yielding a variety of new phenotypes. The lky::Mucts mutation did not give rise to obvious alterations in the gross morphology of the cell or in cell division.

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Role of murein lipoprotein in morphogenesis of the bacterial division septum: phenotypic similarity of lkyD and lpo mutants

Cited by 68 publications

References 6 publications

Plasmolysis induced by toluene in a cyoB mutant of Pseudomonas putida

Plasmolysis induced by toluene in a cyoB mutant of Pseudomonas putida

TolB protein ofEscherichia coliK‐12 interacts with the outer membrane peptidoglycan‐associated proteins Pal, Lpp and OmpA

Defective transport and other phenotypes of a periplasmic "leaky" mutant of Escherichia coli K-12

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