Protein diffusion in Escherichia coli cytoplasm scales with the mass ofthe complexes and is location dependent

Wojciech M. Smigiel, Luca Mantovanelli, Dmitrii S. Linnik, Michiel Punter, Jakob Silberberg, Limin Xiang, Ke Xu, Bert Poolman*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

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Abstract

We analyze the structure of the cytoplasm by performing single-molecule displacement mapping on a diverse set of native cytoplasmic proteins in exponentially growing Escherichia coli. We evaluate the method for application in small compartments and find that confining effects of the cell membrane affect the diffusion maps. Our analysis reveals that protein diffusion at the poles is consistently slower than in the center of the cell, i.e., to an extent greater than the confining effect of the cell membrane. We also show that the diffusion coefficient scales with the mass of the used probes, taking into account the oligomeric state of the proteins, while parameters such as native protein abundance or the number of protein-protein interactions do not correlate with the mobility of the proteins. We argue that our data paint the prokaryotic cytoplasm as a compartment with subdomains in which the diffusion of macromolecules changes with the perceived viscosity.

Original languageEnglish
Article numbereabo5387
Number of pages19
JournalScience Advances
Volume8
Issue number32
DOIs
Publication statusPublished - Aug-2022

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