Much of the molecular motion in the cytoplasm is diffusive, which possibly limits the tempo of processes. We studied the dependence of protein mobility on protein surface properties and ionic strength. We used surface-modified fluorescent proteins (FPs) and determined their translational diffusion coefficients (D) in the cytoplasm of Escherichia coli, Lactococcus lactis and Haloferax volcanii. We find that in E. coli D depends on the net charge and its distribution over the protein, with positive proteins diffusing up to 100-fold slower than negative ones. This effect is weaker in L. lactis and Hfx. volcanii due to electrostatic screening. The decrease in mobility is probably caused by interaction of positive FPs with ribosomes as shown in in vivo diffusion measurements and confirmed in vitro with purified ribosomes. Ribosome surface properties may thus limit the composition of the cytoplasmic proteome. This finding lays bare a paradox in the functioning of prokaryotic (endo)symbionts.
E. coli K12 proteomeproteome ID: UP000000318.
L. lactis sub. cremoris MG1363 proteomeproteome ID: UP000000364.
Hfx. volcanii DS2 proteomeproteome ID: UP000008243.
Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) proteomeproteome ID: UP000001806.
Blochmannia floridanus proteomeproteome ID: UP000002192.
Onion yellows phytoplasma (strain OY-M) proteomeproteome ID: UP000002523.
Wigglesworthia glossinidia brevipalpis proteomeproteome ID: UP000000562.
- Bert Poolman
- Wojciech M Śmigiel
The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication.
- Victor Sourjik, Max Planck Institute for Terrestrial Microbiology, Germany
© 2017, Schavemaker et al.
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