Microdomain formation is a general property of bacterial membrane proteins and induces heterogeneity of diffusion patterns

BMC Biology
Daniella LucenaP L Graumann

Abstract

Proteins within the cytoplasmic membrane display distinct localization patterns and arrangements. While multiple models exist describing the dynamics of membrane proteins, to date, there have been few systematic studies, particularly in bacteria, to evaluate how protein size, number of transmembrane domains, and temperature affect their diffusion, and if conserved localization patterns exist. We have used fluorescence microscopy, single-molecule tracking (SMT), and computer-aided visualization methods to obtain a better understanding of the three-dimensional organization of bacterial membrane proteins, using the model bacterium Bacillus subtilis. First, we carried out a systematic study of the localization of over 200 B. subtilis membrane proteins, tagged with monomeric mVenus-YFP at their original gene locus. Their subcellular localization could be discriminated in polar, septal, patchy, and punctate patterns. Almost 20% of membrane proteins specifically localized to the cell poles, and a vast majority of all proteins localized in distinct structures, which we term microdomains. Dynamics were analyzed for selected membrane proteins, using SMT. Diffusion coefficients of the analyzed transmembrane proteins did not correlate with...Continue Reading

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Citations

May 30, 2020·Proceedings of the National Academy of Sciences of the United States of America·Bing FuPeng Chen
Mar 3, 2020·Frontiers in Microbiology·Hector RomeroJuan C Alonso
May 18, 2021·Frontiers in Microbiology·Benjamin MayerPeter L Graumann

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Methods Mentioned

BETA
fluorescence microscopy
PCR

Software Mentioned

Wolfram Mathematica
MATLAB
SMT
MicrobeTracker
Fiji ImageJ
VisiView
microbe tracker
MinJ
Andor Solis
track

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