Solution Structure of a Bacterial Microcompartment Targeting Peptide and Its Application in the Construction of an Ethanol Bioreactor

Lawrence, Andrew D., Frank, Stefanie, Newnham, Sarah, Lee, Matthew J., Brown, Ian R., Xue, Wei-Feng, Rowe, Michelle L., Mulvihill, Daniel P., Prentice, Michael B., Howard, Mark J., and others. (2014) Solution Structure of a Bacterial Microcompartment Targeting Peptide and Its Application in the Construction of an Ethanol Bioreactor. ACS Synthetic Biology, 3 (7). pp. 454-465. ISSN 2161-5063. (doi:10.1021/sb4001118) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:42019)

The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided.
Official URL: http://dx.doi.org/10.1021/sb4001118

Abstract

Targeting of proteins to bacterial microcompartments (BMCs) is mediated by an 18-amino-acid peptide sequence. Herein, we report the solution structure of the N-terminal targeting peptide (P18) of PduP, the aldehyde dehydrogenase associated with the 1,2-propanediol utilization metabolosome from Citrobacter freundii. The solution structure reveals the peptide to have a well-defined helical conformation along its whole length. Saturation transfer difference and transferred NOE NMR has highlighted the observed interaction surface on the peptide with its main interacting shell protein, PduK. By tagging both a pyruvate decarboxylase and an alcohol dehydrogenase with targeting peptides, it has been possible to direct these enzymes to empty BMCs in vivo and to generate an ethanol bioreactor. Not only are the purified, redesigned BMCs able to transform pyruvate into ethanol efficiently, but the strains containing the modified BMCs produce elevated levels of alcohol.

Item Type:	Article
DOI/Identification number:	10.1021/sb4001118
Uncontrolled keywords:	metabolic engineering; compartmentalization; propanediol utilization; synthetic biology
Subjects:	Q Science Q Science > QH Natural history > QH301 Biology
Divisions:	Divisions > Division of Natural Sciences > Biosciences
Depositing User:	Susan Davies
Date Deposited:	29 Jul 2014 13:20 UTC
Last Modified:	17 Aug 2022 10:57 UTC
Resource URI:	https://kar.kent.ac.uk/id/eprint/42019 (The current URI for this page, for reference purposes)
Lawrence, Andrew D.:	https://orcid.org/0000-0002-5853-5409
Xue, Wei-Feng:	https://orcid.org/0000-0002-6504-0404
Mulvihill, Daniel P.:	https://orcid.org/0000-0003-2502-5274
Warren, Martin J.:	https://orcid.org/0000-0002-6028-6456

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