Bacterial microcompartment-directed polyphosphate kinase promotes stable polyphosphate accumulation in E. coli.
Cast your vote
You can rate an item by clicking the amount of stars they wish to award to this item.
When enough users have cast their vote on this item, the average rating will also be shown.
Your vote was cast
Thank you for your feedback
Thank you for your feedback
MetadataShow full item record
AbstractProcesses for the biological removal of phosphate from wastewater rely on temporary manipulation of bacterial polyphosphate levels by phased environmental stimuli. In E. coli polyphosphate levels are controlled via the polyphosphate-synthesizing enzyme polyphosphate kinase (PPK1) and exopolyphosphatases (PPX and GPPA), and are temporarily enhanced by PPK1 overexpression and reduced by PPX overexpression. We hypothesised that partitioning PPK1 from cytoplasmic exopolyphosphatases would increase and stabilise E. coli polyphosphate levels. Partitioning was achieved by co-expression of E. coli PPK1 fused with a microcompartment-targeting sequence and an artificial operon of Citrobacter freundii bacterial microcompartment genes. Encapsulation of targeted PPK1 resulted in persistent phosphate uptake and stably increased cellular polyphosphate levels throughout cell growth and into the stationary phase, while PPK1 overexpression alone produced temporary polyphosphate increase and phosphate uptake. Targeted PPK1 increased polyphosphate in microcompartments 8-fold compared with non-targeted PPK1. Co-expression of PPX polyphosphatase with targeted PPK1 had little effect on elevated cellular polyphosphate levels because microcompartments retained polyphosphate. Co-expression of PPX with non-targeted PPK1 reduced cellular polyphosphate levels. Thus, subcellular compartmentalisation of a polymerising enzyme sequesters metabolic products from competing catabolism by preventing catabolic enzyme access. Specific application of this process to polyphosphate is of potential application for biological phosphate removal.
CitationBiotechnol J. 2017 Mar;12(3). doi: 10.1002/biot.201600415. Epub 2017 Feb 10
AffiliationHZI, Helmholtz Zentrum für Infektionsforschung GmbH, Inhoffenstr. 7, 38124 Braunschweig Germany.
The following license files are associated with this item:
Except where otherwise noted, this item's license is described as Attribution-NonCommercial-ShareAlike 4.0 International
- Polyphosphate kinase 1 is required for the pathogenesis process of meningitic Escherichia coli K1 (RS218).
- Authors: Peng L, Luo WY, Zhao T, Wan CS, Jiang Y, Chi F, Zhao W, Cao H, Huang SH
- Issue date: 2012 Mar
- Molecular characterization of polyphosphate (PolyP) operon from Serratia marcescens.
- Authors: Lee SJ, Lee YS, Lee YC, Choi YL
- Issue date: 2006
- Polyphosphate metabolism in Escherichia coli.
- Authors: Sharfstein ST, Keasling JD
- Issue date: 1994 Nov 30
- Multi-level evaluation of Escherichia coli polyphosphate related mutants using global transcriptomic, proteomic and phenomic analyses.
- Authors: Varas M, Valdivieso C, Mauriaca C, Ortíz-Severín J, Paradela A, Poblete-Castro I, Cabrera R, Chávez FP
- Issue date: 2017 Apr
- Genetic manipulation of polyphosphate metabolism affects cadmium tolerance in Escherichia coli.
- Authors: Keasling JD, Hupf GA
- Issue date: 1996 Feb