Increased cytoplasm viscosity hampers aggregate polar segregation in Escherichia coli.
In Escherichia coli, under optimal conditions, protein aggregates associated with cellular aging are excluded from midcell by the nucleoid. We study the functionality of this process under sub-optimal temperatures from population and time lapse images of individual cells and aggregates and nucleoids within. We show that, as temperature decreases, aggregates become homogeneously distributed and uncorrelated with nucleoid size and location. We present evidence that this is due to increased cytoplasm viscosity, which weakens the anisotropy in aggregate displacements at the nucleoid borders that is responsible for their preference for polar localisation. Next, we show that in plasmolysed cells, which have increased cytoplasm viscosity, aggregates are also not preferentially located at the poles. Finally, we show that the inability of cells with increased viscosity to exclude aggregates from midcell results in enhanced aggregate concentration in between the nucleoids in cells close to dividing. This weakens the asymmetries in aggregate numbers between sister cells of subsequent generations required for rejuvenating cell lineages. We conclude that the process of exclusion of protein aggregates from midcell is not immune to stress conditions affecting the cytoplasm viscosity. The findings contribute to our understanding of E. coli's internal organisation and functioning, and its fragility to stressful conditions.
Laboratory of Biosystem Dynamics, Department of Signal Processing, Tampere University of Technology, 33101, Tampere, Finland.
Samuel M D
SM
Oliveira
Laboratory of Biosystem Dynamics, Department of Signal Processing, Tampere University of Technology, 33101, Tampere, Finland.
Ramakanth
R
Neeli-Venkata
Laboratory of Biosystem Dynamics, Department of Signal Processing, Tampere University of Technology, 33101, Tampere, Finland.
Nadia S M
NS
Goncalves
UNINOVA, Instituto de Desenvolvimento de Novas Tecnologias, Campus FCT-UNL, 2829-516, Caparica, Portugal.
João A
JA
Santinha
UNINOVA, Instituto de Desenvolvimento de Novas Tecnologias, Campus FCT-UNL, 2829-516, Caparica, Portugal.
Leonardo
L
Martins
Laboratory of Biosystem Dynamics, Department of Signal Processing, Tampere University of Technology, 33101, Tampere, Finland.
Huy
H
Tran
Laboratory of Biosystem Dynamics, Department of Signal Processing, Tampere University of Technology, 33101, Tampere, Finland.
Jarno
J
Mäkelä
Laboratory of Biosystem Dynamics, Department of Signal Processing, Tampere University of Technology, 33101, Tampere, Finland.
Abhishekh
A
Gupta
UNINOVA, Instituto de Desenvolvimento de Novas Tecnologias, Campus FCT-UNL, 2829-516, Caparica, Portugal.
Marilia
M
Barandas
Laboratory of Biosystem Dynamics, Department of Signal Processing, Tampere University of Technology, 33101, Tampere, Finland.
Antti
A
Häkkinen
Laboratory of Biosystem Dynamics, Department of Signal Processing, Tampere University of Technology, 33101, Tampere, Finland.
Jason
J
Lloyd-Price
UNINOVA, Instituto de Desenvolvimento de Novas Tecnologias, Campus FCT-UNL, 2829-516, Caparica, Portugal.
José M
JM
Fonseca
Laboratory of Biosystem Dynamics, Department of Signal Processing, Tampere University of Technology, 33101, Tampere, Finland.
Andre S
AS
Ribeiro
D002455:Cell Division; D003593:Cytoplasm / Q000737:chemistry* / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000502:physiology*; D015388:Organelles / Q000378:metabolism; D066329:Protein Aggregates; D013312:Stress, Physiological; D013696:Temperature; D014783:Viscosity
D029968:Escherichia coli Proteins; D066329:Protein Aggregates