How big is the periplasmic space?

Wielink, John E. van; Duine, Johannis A.

doi:10.1016/0968-0004(90)90208-s

Cited by 57 publications

(21 citation statements)

References 9 publications

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“…If the ␣-helical domain exists as a single, uninterrupted 230-residue ␣ helix, it would be nearly 35 nm in length (1.5 Å rise/residue). An ␣-helix of this length could be accommodated if the periplasm were as wide (between 30 and 70 nm) as that predicted by several studies (19,38). Alternatively, the ␣-helical domain of TolA may be arranged as a bundle of several ␣ helices and localized at the adhesion zones of the cell envelope (15) where the width of the periplasmic space would be narrowed considerably.…”

Section: Discussionmentioning

confidence: 82%

The TolA protein interacts with colicin E1 differently than with other group A colicins

1997

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The 421-residue protein TolA is required for the translocation of group A colicins (colicins E1, E2, E3, A, K, and N) across the cell envelope of Escherichia coli. Mutations in TolA can render cells tolerant to these colicins and cause hypersensitivity to detergents and certain antibiotics, as well as a tendency to leak periplasmic proteins. TolA contains a long ␣-helical domain which connects a membrane anchor to the C-terminal domain, which is required for colicin sensitivity. The functional role of the ␣-helical domain was tested by deletion of residues 56 to 169 (TolA⌬1), 166 to 287 (TolA⌬2), or 54 to 287 (TolA⌬3) of the ␣-helical domain of TolA, which removed the N-terminal half, the C-terminal half, or nearly the entire ␣-helical domain of TolA, respectively. TolA and TolA deletion mutants were expressed from a plasmid in an E. coli strain producing no chromosomally encoded TolA. Cellular sensitivity to the detergent deoxycholate was increased for each deletion mutant, implying that more than half of the TolA ␣-helical domain is necessary for cell envelope stability. Removal of either the N-or C-terminal half of the ␣-helical domain resulted in a slight (ca. 5-fold) decrease in cytotoxicity of the TolA-dependent colicins A, E1, E3, and N compared to cells producing wild-type TolA when these mutants were expressed alone or with TolQ, -R, and -B. In cells containing TolA⌬3, the cytotoxicity of colicins A and E3 was decreased by a factor of >3,000, and K ؉ efflux induced by colicins A and N was not detectable. In contrast, for colicin E1 action on TolA⌬3 cells, there was little decrease in the cytotoxic activity (<5-fold) or the rate of K ؉ efflux, which was similar to that from wild-type cells. It was concluded that the mechanism(s) by which cellular uptake of colicin E1 is mediated by the TolA protein differs from that for colicins A, E3, and N. Possible explanations for the distinct interaction and unique translocation mechanism of colicin E1 are discussed.

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Section: Discussionmentioning

confidence: 82%

The TolA protein interacts with colicin E1 differently than with other group A colicins

1997

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“…This observation suggests that the "reach" of the T6SS is about half the width of the bacterial cell, a sufficient distance to possibly penetrate through the entire cell envelop of a target cell that is in close proximity. In fact, given that the thickness of the periplasmic space is roughly 10-25 nm (22), while the width of the whole cell is roughly 500 nm, the periplasmic space only occupies ∼5% of the potential target space of any given T6SS attack, suggesting that the cytosol is the most likely repository of T6SS-delivered effectors. However, the only effector found in V. cholerae with a clearly identified bacterial target is the peptidoglycan-degrading VgrG3 effector, which has a periplasmic substrate.…”

Section: Resultsmentioning

confidence: 99%

Vibrio cholerae type 6 secretion system effector trafficking in target bacterial cells

Dong

et al. 2017

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

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The type 6 secretion system (T6SS) is used by many Gram-negative bacterial species to deliver toxic effector proteins into nearby bacteria prey cells to kill or inhibit their growth. VgrG proteins are core conserved secretion substrates of the T6SS and one subset of T6SS effectors consists of VgrG proteins with C-terminal extension domains carrying various enzymatic activities. In Vibrio cholerae, VgrG3 has a hydrolase extension domain and degrades peptidoglycan in the periplasm of target bacteria. In this study, we replaced this domain with a nuclease domain from Salmonella enterica subsp. arizonae. This modified V. cholerae strain was able to kill its parent using its T6SS. This result also demonstrated that V. cholerae T6SS is capable of delivering effectors that could attack substrates found either in the periplasm or cytosol of target bacteria. Additionally, we found that effectors VgrG3 and TseL, despite lacking a classical Sec or TAT secretion signal, were able to reach the periplasm when expressed in the bacterial cytosol. This effector trafficking likely represents an evolutionary strategy for T6SS effectors to reach their intended substrates regardless of which subcellular compartment in the target cell they happen to be delivered to by the T6SS apparatus.

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“…If the periplasm is on average 7.5 nm wide, this would give the volume of the periplasm of a single cell as 6 x L. If there is a maximum of 2.4 nmol maltose transported by 10' cells per minute, a rate of 0.0067 M s" is obtained as an approximation for the absolute V,,, of transport. This value might, however, be lower if alternate values of the periplasmic dimensions (Oliver, 1987;van Wielink & Duine, 1990) are used. It might also be higher if the entire volume of the periplasm is not available, as for example if the transport systems are clustered at the poles of the cells as is suggested by the data of Maddock and Shapiro (1993).…”

Section: Absolute Velocitymentioning

confidence: 99%

Simple models for the analysis of binding protein‐dependent transport systems

Shilton

Mowbray

1995

Protein Science

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Mathematical modeling was used to evaluate experimental data for bacterial binding protein-dependent transport systems. Two simple models were considered in which ligand-free periplasmic binding protein interacts with the membrane-bound components of transport. In one, this interaction was viewed as a competition with the ligandbound binding protein, whereas in the other, it was considered to be a consequence of the complexes formed during the transport process itself. Two sets of kinetic parameters were derived for each model that fit the available experimental results for the maltose system. By contrast, a model that omitted the interaction of ligand-free binding protein did not fit the experimental data. Some applications of the successful models for the interpretation of existing mutant data are illustrated, as well as the possibilities of using mutant data to test the original models and sets of kinetic parameters. Practical suggestions are given for further experimental design.

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How big is the periplasmic space?

Cited by 57 publications

References 9 publications

The TolA protein interacts with colicin E1 differently than with other group A colicins

The TolA protein interacts with colicin E1 differently than with other group A colicins

Vibrio cholerae type 6 secretion system effector trafficking in target bacterial cells

Simple models for the analysis of binding protein‐dependent transport systems

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