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Membrane curvature and the Tol-Pal complex determine polar localization of the chemoreceptor Tar in E. coli

Terrens N. V. Saaki, Henrik Strahl, View ORCID ProfileLeendert W. Hamoen
doi: https://doi.org/10.1101/212670
Terrens N. V. Saaki
1Swammerdam Institute for Life Sciences, University of Amsterdam, Science Park 904, 1098 XH Amsterdam, The Netherlands
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Henrik Strahl
2Centre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle NE2 4AX, United Kingdom
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Leendert W. Hamoen
1Swammerdam Institute for Life Sciences, University of Amsterdam, Science Park 904, 1098 XH Amsterdam, The Netherlands
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  • ORCID record for Leendert W. Hamoen
  • For correspondence: l.w.hamoen@uva.nl
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Abstract

Chemoreceptors are localized at the cell poles of Escherichia coli and other rod-shaped bacteria. Over the years different mechanisms have been put forward to explain this polar localization; from stochastic clustering, membrane curvature driven localization, interactions with the Tol-Pal complex, to nucleoid exclusion. To evaluate these mechanisms, we monitored the cellular localization of the aspartate chemoreceptor Tar in different deletion mutants. We did not find any indication for either stochastic cluster formation or nucleoid exclusion. However, the presence of a functional Tol-Pal complex appeared to be essential to retain Tar at cell poles. This finding also implies that the curvature of cell poles does not attract chemoreceptor complexes. Interestingly, Tar still accumulated at midcell in tol and in pal deletion mutants. In these mutants, the protein appears to gather at the base of division septa, a region characterised by strong membrane curvature. Chemoreceptors, like Tar, form trimer-of-dimers that bend the cell membrane due to a rigid tripod structure with an estimated curvature of approximately 37 nm. This curvature approaches the curvature of the cell membrane generated during cell division, and localization of chemoreceptor tripods at curved membrane areas is therefore energetically favourable as it lowers membrane tension. Indeed, when we introduced mutations in Tar that abolish the rigid tripod structure, the protein was no longer able to accumulate at midcell or cell poles. These findings favour a model where chemoreceptor localization in E. coli is driven by strong membrane curvature and association with the Tol-Pal complex.

Importance Bacteria have exquisite mechanisms to sense and to adapt to the environment they live in. One such mechanism involves the chemotaxis signal transduction pathway, in which chemoreceptors specifically bind certain attracting or repelling molecules and transduce the signals to the cell. In different rod-shaped bacteria, these chemoreceptors localize specifically to cell poles. Here, we examined the polar localization of the aspartate chemoreceptor Tar in E. coli, and found that membrane curvature at cell division sites and interaction with the Tal-pol protein complex, localize Tar at cell division sites, the future cell poles. This study shows how membrane curvature can guide localization of proteins in a cell.

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Posted November 01, 2017.
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Membrane curvature and the Tol-Pal complex determine polar localization of the chemoreceptor Tar in E. coli
Terrens N. V. Saaki, Henrik Strahl, Leendert W. Hamoen
bioRxiv 212670; doi: https://doi.org/10.1101/212670
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Membrane curvature and the Tol-Pal complex determine polar localization of the chemoreceptor Tar in E. coli
Terrens N. V. Saaki, Henrik Strahl, Leendert W. Hamoen
bioRxiv 212670; doi: https://doi.org/10.1101/212670

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