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Solution structure of a bacterial microcompartment targeting peptide and its application in the construction of an ethanol bioreactor

Howard, M (2014) Solution structure of a bacterial microcompartment targeting peptide and its application in the construction of an ethanol bioreactor. ACS Chemical Biology, 3 (7). pp. 454-465. ISSN 1554-8929. E-ISSN 1554-8937. (doi:10.1021/sb4001118) (KAR id:54614)

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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 > QD Chemistry > QD431 Organic Chemistry- Biochemistry- Proteins, peptides, amino acids
Divisions: Faculties > Sciences > School of Biosciences > Protein Science Group
Depositing User: M.J. Howard
Date Deposited: 23 Mar 2016 17:11 UTC
Last Modified: 29 May 2019 17:07 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/54614 (The current URI for this page, for reference purposes)
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