ArticlePloS one2012
Fluorescence correlation spectroscopy measurements of the membrane protein TetA in Escherichia coli suggest rapid diffusion at short length scales.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- In-Depth Study of Low-Complexity Domains: From Structural Diversity to Disease Mechanisms.Cells · 2025Review
- A Live Bacterial Screening Assay for Membrane-Active Antimicrobial Compounds Using Imaging Fluorescence Correlation Spectroscopy.Analytical chemistry · 2025Article
- Space and time on the membrane: modelling Type VI secretion system dynamics as a state-dependent random walk.Royal Society open science · 2023Article
- Bacterial Vivisection: How Fluorescence-Based Imaging Techniques Shed a Light on the Inner Workings of Bacteria.Microbiology and molecular biology reviews : MMBR · 2020Review
- Microdomain formation is a general property of bacterial membrane proteins and induces heterogeneity of diffusion patterns.BMC biology · 2018Article
- How Important Is Protein Diffusion in Prokaryotes?Frontiers in molecular biosciences · 2018Review
- On the Equivalence of FCS and FRAP: Simultaneous Lipid Membrane Measurements.Biophysical journal · 2016Article
- MreB-Dependent Organization of the E. coli Cytoplasmic Membrane Controls Membrane Protein Diffusion.Biophysical journal · 2016Article
- Focal Targeting of the Bacterial Envelope by Antimicrobial Peptides.Frontiers in cell and developmental biology · 2016Review
- Direct live imaging of cell-cell protein transfer by transient outer membrane fusion in Myxococcus xanthus.eLife · 2013Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Structural inhomogeneities in biomembranes can lead to complex diffusive behavior of membrane proteins that depend on the length or time scales that are probed. This effect is well studied in eukaryotic cells, but has been explored only recently in bacteria. Here we used fluorescence recovery after photobleaching (FRAP) and fluorescence correlation spectroscopy (FCS) to study diffusion of the membrane protein TetA-YFP in E. coli. We find that the diffusion constant determined from FRAP is comparable to other reports of inner membrane protein diffusion constants in E. coli. However, FCS, which probes diffusion on shorter length scales, gives a value that is almost two orders of magnitude higher and is comparable to lipid diffusion constants. These results suggest there is a population of TetA-YFP molecules in the membrane that move rapidly over short length scales (~ 400 nm) but move significantly more slowly over the longer length scales probed by FRAP.
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Registered trials
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