Bacterial microcompartment-directed polyphosphate kinase promotes stable polyphosphate accumulation in E. coli

dc.check.date2018-02-10
dc.check.infoAccess to this article is restricted until 12 months after publication at the request of the publisher.en
dc.contributor.authorLiang, Mingzhi
dc.contributor.authorFrank, Stefanie
dc.contributor.authorLünsdorf, Heinrich
dc.contributor.authorWarren, Martin J.
dc.contributor.authorPrentice, Michael B.
dc.contributor.funderHealth Research Boarden
dc.contributor.funderScience Foundation Irelanden
dc.contributor.funderBiotechnology and Biological Sciences Research Councilen
dc.date.accessioned2017-07-04T09:13:34Z
dc.date.available2017-07-04T09:13:34Z
dc.date.issued2017-02-10
dc.date.updated2017-07-03T16:19:16Z
dc.description.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.en
dc.description.sponsorshipHealth Research Board (award HRA_POR/2011/111); Science Foundation Ireland (SFI Grant Numbers 11/TIDA/B2001 and SFI/12/RC/2273); British Biotechnology and Biological Sciences Research Council (BB/M002969 and BB/H013180)en
dc.description.statusPeer revieweden
dc.description.versionAccepted Versionen
dc.format.mimetypeapplication/pdfen
dc.identifier.articleid1600415
dc.identifier.citationLiang, M., Frank, S., Lünsdorf, H., Warren, M. J. and Prentice, M. B. (2017) 'Bacterial microcompartment-directed polyphosphate kinase promotes stable polyphosphate accumulation in E. coli', Biotechnology Journal, 12(3), 1600415en
dc.identifier.doi10.1002/biot.201600415
dc.identifier.endpage1600415en
dc.identifier.issn1860-6768
dc.identifier.issued3en
dc.identifier.journaltitleJournal of Biotechnologyen
dc.identifier.startpage1600415en
dc.identifier.urihttps://hdl.handle.net/10468/4211
dc.identifier.volume12en
dc.language.isoenen
dc.publisherWiley-VCH Verlagen
dc.rightsThis is the accepted version of the following article: Liang et al (2017), Bacterial microcompartment-directed polyphosphate kinase promotes stable polyphosphate accumulation in E. coli. Biotechnol. J., 12: 1600415 which has been published in final form at http://dx.doi.org/10.1002/biot.201600415 .This article may be used for non-commercial purposes in accordance with the Wiley Self-Archiving Policy [olabout.wiley.com/WileyCDA/Section/id-820227.html]en
dc.subjectBacteriaen
dc.subjectBiopolymersen
dc.subjectMetabolic engineeringen
dc.subjectMicroreactorsen
dc.subjectSynthetic biologyen
dc.subjectEscherichia colien
dc.subjectInorganic polyphosphateen
dc.subjectWaste wateren
dc.subjectSalmonella entericaen
dc.subjectProteinen
dc.subjectPhosphateen
dc.subjectGeneen
dc.subjectMetabolismen
dc.subjectOrganellesen
dc.subjectSequencesen
dc.titleBacterial microcompartment-directed polyphosphate kinase promotes stable polyphosphate accumulation in E. colien
dc.typeArticle (peer-reviewed)en
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