Protein diffusion in Escherichia coli cytoplasm scales with the mass of the complexes and is location dependent.
Wojciech Mikołaj ŚmigielLuca MantovanelliDmitrii S LinnikMichiel PunterJakob M SilberbergLimin XiangKe XuBert PoolmanPublished in: Science advances (2022)
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.
Keyphrases
- single molecule
- escherichia coli
- protein protein
- depressive symptoms
- binding protein
- high resolution
- small molecule
- atomic force microscopy
- single cell
- biofilm formation
- magnetic resonance imaging
- mental health
- stem cells
- cell therapy
- big data
- staphylococcus aureus
- mesenchymal stem cells
- cystic fibrosis
- klebsiella pneumoniae
- artificial intelligence