Aggregation of Escherichia coli proteins during stationary phase depends on glucose and oxygen availability

Kwiatkowska, J; Matuszewska, Ewelina; Kuczyńska-Wiśnik, Dorota; Laskowska, Ewa

doi:10.1016/j.resmic.2008.09.008

Cited by 36 publications

(33 citation statements)

References 27 publications

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“…Apparently, stress levels did influence this aggregation capability because the cells with more toxic ENPs of NiO formed bigger flocs than those with CuO . This phenomenon is consistent with the fact that environmental stresses trigger expression of proteins to induce cell aggregation (Kwiatkowska et al, 2008). Bacteria also have other protective responses to environmental stresses .…”

Section: Response Of Soil Microorganisms To Enpssupporting

confidence: 83%

Engineered nanoparticles in the soil and their potential implications to microbial activity

et al. 2012

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Section: Response Of Soil Microorganisms To Enpssupporting

confidence: 83%

Engineered nanoparticles in the soil and their potential implications to microbial activity

et al. 2012

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“…However, it is not excluded that the observed effect can depend on an overproduced recombinant protein. To extend our studies, we investigated the effect of Δ cobB and Δ ackA - pta mutations on the aggregation of endogenous E. coli proteins during the late stationary phase [28]. In this experiment, we used LB supplemented with 0.4% glucose to stimulate protein acetylation [16].…”

Section: Resultsmentioning

confidence: 99%

The effect of protein acetylation on the formation and processing of inclusion bodies and endogenous protein aggregates in Escherichia coli cells

Kuczyńska-Wiśnik

Moruno-Algara

Stojowska-Swędrzyńska

et al. 2016

Microb Cell Fact

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BackgroundAcetylation of lysine residues is a reversible post-translational modification conserved from bacteria to humans. Several recent studies have revealed hundreds of lysine-acetylated proteins in various bacteria; however, the physiological role of these modifications remains largely unknown. Since lysine acetylation changes the size and charge of proteins and thereby may affect their conformation, we assumed that lysine acetylation can stimulate aggregation of proteins, especially for overproduced recombinant proteins that form inclusion bodies.ResultsTo verify this assumption, we used Escherichia coli strains that overproduce aggregation-prone VP1GFP protein. We found that in ΔackA-pta cells, which display diminished protein acetylation, inclusion bodies were formed with a delay and processed faster than in the wild-type cells. Moreover, in ΔackA-pta cells, inclusion bodies exhibited significantly increased specific GFP fluorescence. In CobB deacetylase-deficient cells, in which protein acetylation was enhanced, the formation of inclusion bodies was increased and their processing was significantly inhibited. Similar results were obtained with regard to endogenous protein aggregates formed during the late stationary phase in ΔackA-pta and ΔcobB cells.ConclusionsOur studies revealed that protein acetylation affected the aggregation of endogenous E. coli proteins and the yield, solubility, and biological activity of a model recombinant protein. In general, decreased lysine acetylation inhibited the formation of protein aggregates, whereas increased lysine acetylation stabilized protein aggregates. These findings should be considered during the designing of efficient strategies for the production of recombinant proteins in E. coli cells.Electronic supplementary materialThe online version of this article (doi:10.1186/s12934-016-0590-8) contains supplementary material, which is available to authorized users.

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“…To isolate protein aggregates, E. chaffeensis cells were lysed by sonication as described previously (Kwiatkowska et al 2008). The sample volume was adjusted to normalize for the number of bacterial cells in each sample.…”

Section: Isolation Of Protein Aggregatesmentioning

confidence: 99%

Protein aggregation in Ehrlichia chaffeensis during infection of mammalian cells

Kuczyńska-Wiśnik

Cheng

Ganta

et al. 2017

FEMS Microbiology Letters

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One sentence summary: The proteome of an intracellular pathogen Ehrlichia chaffeensis becomes aggregation-prone during infection of mammalian cells. Editor: Akio Nakane ABSTRACTEhrlichia chaffeensis is an obligatory intracellular pathogen transmitted through infected ticks to humans and other vertebrates. We investigated the extent of protein aggregation in E. chaffeensis during infection of canine macrophage cell line, DH82. We discovered that the size of the aggregated fraction of E. chaffeensis proteins increased during the first 48 h post infection. We also incubated the infected cells with guanidinium chloride (GuHCl), a known inhibitor of the protein-disaggregating molecular chaperone ClpB. Up to 0.5 mM GuHCl had no impact on the host cells, whereas the viability of the pathogen was reduced by ∼60% in the presence of the inhibitor. Furthermore, we found that the size of the aggregated protein fraction in E. chaffeensis increased significantly in cultures supplemented with 0.5 mM GuHCl, which also resulted in the preferential accumulation of ClpB with the aggregated proteins. Altogether, our results suggest that an exposure of E. chaffeensis to the stressful environment of a host cell results in an increased aggregation of the pathogen's proteins, which is exacerbated upon inhibition of ClpB. Our studies establish a link between protein quality control and pathogen survival during infection of a host.

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Aggregation of Escherichia coli proteins during stationary phase depends on glucose and oxygen availability

Cited by 36 publications

References 27 publications

Engineered nanoparticles in the soil and their potential implications to microbial activity

Engineered nanoparticles in the soil and their potential implications to microbial activity

The effect of protein acetylation on the formation and processing of inclusion bodies and endogenous protein aggregates in Escherichia coli cells

Protein aggregation in Ehrlichia chaffeensis during infection of mammalian cells

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