General Protein Diffusion Barriers Create Compartments within Bacterial Cells
Abstract
In eukaryotes, the differentiation of cellular extensions such as cilia or neuronal axons depends on the partitioning of proteins to distinct plasma membrane domains by specialized diffusion barriers. However, examples of this compartmentalization strategy are still missing for prokaryotes, although complex cellular architectures are also widespread among this group of organisms. This study reveals the existence of a protein-mediated membrane diffusion barrier in the stalked bacterium Caulobacter crescentus. We show that the Caulobacter cell envelope is compartmentalized by macromolecular complexes that prevent the exchange of both membrane and soluble proteins between the polar stalk extension and the cell body. The barrier structures span the cross-sectional area of the stalk and comprise at least four proteins that assemble in a cell-cycle-dependent manner. Their presence is critical for cellular fitness because they minimize the effective cell volume, allowing faster adaptation to environmental changes that require de novo synthesis of envelope proteins.
Additional Information
© 2012 Elsevier Inc. Received: March 19, 2012. Revised: July 24, 2012. Accepted: October 14, 2012. Published online: November 29, 2012. We thank Stephanie Wick for excellent technical assistance; Nikolay Ouzounov for helpful discussions; Juliane Kühn, Patrick Viollier, and Grant Bowman for providing plasmids and strains; and Sarah Cheng for help with image segmentation. This work was supported by funds from the Max Planck Society to M.T., a Young Investigator Grant (RGY0069/2008-C) from the Human Frontier Science Program to Z.G. and M.T., a National Institutes of Health (NIH) Director's New Innovator Award (DP2OD004389) to Z.G., an NRSA postdoctoral fellowship (F32GM906842) from the National Institute of General Medical Sciences to E.A.K., NIH grant GM51986 to Y.V.B, and NIH grant RO1GM094800B to G.J.J.Attached Files
Accepted Version - nihms428421.pdf
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Additional details
- PMCID
- PMC3542395
- Eprint ID
- 36171
- DOI
- 10.1016/j.cell.2012.10.046
- Resolver ID
- CaltechAUTHORS:20130104-105656715
- Max Planck Society
- Human Frontier Science Program
- RGY0069/2008-C
- NIH
- DP2OD004389
- NIH Postdoctoral Fellowship
- F32GM906842
- NIH
- GM51986
- NIH
- RO1GM094800B
- Created
-
2013-01-04Created from EPrint's datestamp field
- Updated
-
2021-11-09Created from EPrint's last_modified field