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Title: Asymmetric polar localization dynamics of the serine chemoreceptor protein Tsr in Escherichia coli
Authors: Oh D. 
Yu Y.
Lee H.
Jeon J.-H.
Wanner B.L.
Ritchie K.
Keywords: bacterial protein
serine chemorecptor protein Tsr
unclassified drug
methyl accepting chemotaxis protein
tsr protein, E coli
cluster analysis
Escherichia coli
fluorescence analysis
image analysis
protein localization
protein stability
protein synthesis
protein transport
Escherichia coli
molecular imaging
Escherichia coli
Methyl-Accepting Chemotaxis Proteins
Molecular Imaging
Protein Transport
Issue Date: 2018
Citation: Oh D., Yu Y., Lee H., Jeon J.-H., Wanner B.L., Ritchie K. (2018). Asymmetric polar localization dynamics of the serine chemoreceptor protein Tsr in Escherichia coli. PLoS ONE 13 (5) : e0195887. ScholarBank@NUS Repository.
Rights: Attribution 4.0 International
Abstract: The spatial location of proteins in living cells can be critical for their function. For example, the E. coli chemotaxis machinery is localized to the cell poles. Here we describe the polar localization of the serine chemoreceptor Tsr using a strain synthesizing a fluorescent Tsr-Venus fusion at a low level from a single-copy chromosomal construct. Using photobleaching and imaging during recovery by new synthesis, we observed distinct asymmetry between a bright (old) pole and a dim (new) pole. The old pole was shown to be a more stable cluster and to recover after photobleaching faster, which is consistent with the hypothesis that newly synthesized Tsr proteins are inserted directly at or near the old pole. The new pole was shown to be a less stable cluster and to exchange proteins freely with highly mobile Tsr-Venus proteins diffusing in the membrane. We propose that the new pole arises from molecules escaping from the old pole and diffusing to the new pole where a more stable cluster forms over time. Our localization imaging data support a model in which a nascent new pole forms prior to stable cluster formation. © 2018 Oh et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Source Title: PLoS ONE
ISSN: 19326203
DOI: 10.1371/journal.pone.0195887
Rights: Attribution 4.0 International
Appears in Collections:Staff Publications

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