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

Show simple item record Liang, Mingzhi Frank, Stefanie Lünsdorf, Heinrich Warren, Martin J. Prentice, Michael B. 2017-07-04T09:13:34Z 2017-07-04T09:13:34Z 2017-02-10
dc.identifier.citation Liang, 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), 1600415 en
dc.identifier.volume 12 en
dc.identifier.issued 3 en
dc.identifier.startpage 1600415 en
dc.identifier.endpage 1600415 en
dc.identifier.issn 1860-6768
dc.identifier.doi 10.1002/biot.201600415
dc.description.abstract Processes 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.sponsorship Health 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.format.mimetype application/pdf en
dc.language.iso en en
dc.publisher Wiley-VCH Verlag en
dc.rights This 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 .This article may be used for non-commercial purposes in accordance with the Wiley Self-Archiving Policy [] en
dc.subject Bacteria en
dc.subject Biopolymers en
dc.subject Metabolic engineering en
dc.subject Microreactors en
dc.subject Synthetic biology en
dc.subject Escherichia coli en
dc.subject Inorganic polyphosphate en
dc.subject Waste water en
dc.subject Salmonella enterica en
dc.subject Protein en
dc.subject Phosphate en
dc.subject Gene en
dc.subject Metabolism en
dc.subject Organelles en
dc.subject Sequences en
dc.title Bacterial microcompartment-directed polyphosphate kinase promotes stable polyphosphate accumulation in E. coli en
dc.type Article (peer-reviewed) en
dc.internal.authorcontactother Michael Prentice, Pathology, University College Cork, Cork, Ireland. +353-21-490-3000 Email: en
dc.internal.availability Full text available en Access to this article is restricted until 12 months after publication at the request of the publisher. en 2018-02-10 2017-07-03T16:19:16Z
dc.description.version Accepted Version en
dc.internal.rssid 400214311
dc.internal.wokid WOS:000398036900009
dc.contributor.funder Health Research Board en
dc.contributor.funder Science Foundation Ireland en
dc.contributor.funder Biotechnology and Biological Sciences Research Council en
dc.description.status Peer reviewed en
dc.identifier.journaltitle Journal of Biotechnology en
dc.internal.copyrightchecked No !!CORA!! en
dc.internal.licenseacceptance Yes en
dc.internal.IRISemailaddress en
dc.identifier.articleid 1600415

Files in this item

This item appears in the following Collection(s)

Show simple item record

This website uses cookies. By using this website, you consent to the use of cookies in accordance with the UCC Privacy and Cookies Statement. For more information about cookies and how you can disable them, visit our Privacy and Cookies statement