Protein Localization in
            <i>Escherichia coli</i>
            Cells: Comparison of the Cytoplasmic Membrane Proteins ProP, LacY, ProW, AqpZ, MscS, and MscL

Romantsov, Tatyana; Battle, Andrew R.; Hendel, Jenifer L.; Martinac, Boris; Wood, Janet M.

doi:10.1128/jb.00967-09

Cited by 110 publications

(102 citation statements)

References 71 publications

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“…The polar localization of CL at regions of negative curvature in spheroplast membranes confirms observations by several groups studying CL-protein interactions in E. coli (18,20) and lipid domain organization in B. subtilis (17,46). The data provide in vivo experimental support for the models described by Wingreen and coworkers (21,22).…”

Section: Discussionsupporting

confidence: 87%

“…Osmotic forces that pin the membrane against the peptidoglycan layer of the cell wall regulate the size of the microdomains. These simulations are supported by recent experiments that suggest CL domains may be responsible for polar protein localization in E. coli cells (20).…”

supporting

confidence: 80%

“…(iii) CL increases the binding efficiency of MinD to liposomes in vitro (41). (iv) CL influences the polar localization of ProP and MscS in E. coli cells in vivo (20).…”

Section: Resultsmentioning

confidence: 99%

“…Many E. coli proteins, including ProP, MscS, MscL, LacY, MinC, and MinD, have been reported to localize to the poles and septa (14,15,20,33,34). We used MinD as a model system to test the effect of membrane curvature on protein localization using the technique of confining spheroplasts in microchambers.…”

Section: Resultsmentioning

confidence: 99%

“…CL is distributed between the two leaflets of the bilayers and is located preferentially at the poles and septa in rod-shaped cells of E. coli, B. subtilis, and Pseudomonas putida (17)(18)(19). The polar positioning of the proline transporter ProP and the mechanosensitive ion channel of small conductance MscS in E. coli is dependent on CL (20). These observations suggest that cell shape may influence the localization of CL and proteins.…”

mentioning

confidence: 91%

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Cardiolipin microdomains localize to negatively curved regions of Escherichia coli membranes

Renner¹,

Weibel

2011

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

314

336

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Many proteins reside at the cell poles in rod-shaped bacteria. Several hypotheses have drawn a connection between protein localization and the large cell-wall curvature at the poles. One hypothesis has centered on the formation of microdomains of the lipid cardiolipin (CL), its localization to regions of high membrane curvature, and its interaction with membrane-associated proteins. A lack of experimental techniques has left this hypothesis unanswered. This paper describes a microtechnology-based technique for manipulating bacterial membrane curvature and quantitatively measuring its effect on the localization of CL and proteins in cells. We confined Escherichia coli spheroplasts in microchambers with defined shapes that were embossed into a layer of polymer and observed that the shape of the membrane deformed predictably to accommodate the walls of the microchambers. Combining this technique with epifluorescence microscopy and quantitative image analyses, we characterized the localization of CL microdomains in response to E. coli membrane curvature. CL microdomains localized to regions of high intrinsic negative curvature imposed by microchambers. We expressed a chimera of yellow fluorescent protein fused to the N-terminal region of MinD-a spatial determinant of E. coli division plane assembly-in spheroplasts and observed its colocalization with CL to regions of large, negative membrane curvature. Interestingly, the distribution of MinD was similar in spheroplasts derived from a CL synthase knockout strain. These studies demonstrate the curvature dependence of CL in membranes and test whether these structures participate in the localization of MinD to regions of negative curvature in cells.A central question in cell biology is how the spatial organization of proteins and lipids is established, maintained, and replicated and how it fluctuates in response to external stimuli. Eukaryotic cells use several mechanisms to accomplish this task, including a dynamic cytoskeleton that controls the spatial and temporal position of proteins, nucleic acid, and organelles (1). The formation of lipid microdomains in the membrane also is involved in the localization of integral membrane proteins (2). These mechanisms play a critical role in cell physiology and behavior.Bacteria also use mechanisms for controlling the intracellular location of proteins, lipids, and nucleic acid. The persistent historical view of bacterial cells as lacking spatial control over their intracellular components inhibited the field. Bacteria are sophisticated organisms that use tightly regulated physiological mechanisms similar to many of those used by eukaryotic cells, including controlling shape, regulating growth and division, transporting intracellular components (e.g., proteins, plasmids, DNA, and RNA), and polarizing the cell (3, 4). These organisms have several remarkable structural characteristics, but one of the most fundamental questions in this area of microbiology-how cells produce, maintain, and replicate their spatial organization-still...

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Section: Discussionsupporting

confidence: 87%

supporting

confidence: 80%

“…(iii) CL increases the binding efficiency of MinD to liposomes in vitro (41). (iv) CL influences the polar localization of ProP and MscS in E. coli cells in vivo (20).…”

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 91%

See 3 more Smart Citations

Cardiolipin microdomains localize to negatively curved regions of Escherichia coli membranes

Renner¹,

Weibel

2011

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

314

336

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Tat transport in Escherichia coli requires zwitterionic phosphatidylethanolamine but no specific negatively charged phospholipid

et al. 2017

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Translocation of folded proteins by the Tat system of Escherichia coli is believed to rely on the presence of phosphatidylethanolamine (PE) and the negatively charged phospholipids cardiolipin (CL) and phosphatidylglycerol (PG). Here we show that while PE is indeed essential for activity, the Tat system is fully functional in a clsA/clsB/clsC deletion strain lacking CL, and in a pgsA deletion strain lacking both PG and CL during aerobic growth on complex media. In contrast to early studies that relied on strains with reduced lipid levels, this study therefore demonstrates that PG and CL are dispensable for Tat transport. The lack of these lipids may be compensated by other anionic phospholipids such as phosphatidic acid, CDP-diacylglycerol, or N-acyl-PE.

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Evolutionarily conserved mechanism for membrane recognition from bacteria to mitochondria

2021

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The mechanisms controlling membrane recognition by proteins with one hydrophobic stretch at their carboxyl terminus (tail anchor, TA) are poorly defined. The Escherichia coli TAs of ElaB and YqjD, which share sequential and structural similarity with the Saccharomyces cerevisiae TA of Fis1, were shown to localize to mitochondria. We show that YqjD and ElaB are directed by their TAs to bacterial cell poles. Fis1(TA) expressed in E. coli localizes like the endogenous TAs. The yeast and bacterial TAs are inserted in the E. coli inner membrane, and they all show affiliation to phosphatidic acid (PA), found in the membrane of the bacterial cell poles and of the yeast mitochondria. Our results suggest a mechanism for TA membrane recognition conserved from bacteria to mitochondria and raise the possibility that through their interaction with PA, and TAs play a role across prokaryotes and eukaryotes in controlling cell/organelle fate.

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Protein Localization in Escherichia coli Cells: Comparison of the Cytoplasmic Membrane Proteins ProP, LacY, ProW, AqpZ, MscS, and MscL

Cited by 110 publications

References 71 publications

Cardiolipin microdomains localize to negatively curved regions of Escherichia coli membranes

Cardiolipin microdomains localize to negatively curved regions of Escherichia coli membranes

Tat transport in Escherichia coli requires zwitterionic phosphatidylethanolamine but no specific negatively charged phospholipid

Evolutionarily conserved mechanism for membrane recognition from bacteria to mitochondria

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