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*

*Bijbehorende auteur voor dit werk

OnderzoeksoutputAcademicpeer review

18 Citaten (Scopus)
199 Downloads (Pure)


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.

Originele taal-2English
Aantal pagina's19
TijdschriftScience Advances
Nummer van het tijdschrift32
StatusPublished - aug.-2022

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