期刊
ACS SYNTHETIC BIOLOGY
卷 3, 期 7, 页码 454-465出版社
AMER CHEMICAL SOC
DOI: 10.1021/sb4001118
关键词
metabolic engineering; compartmentalization; propanediol utilization; synthetic biology
资金
- Biotechnology and Biological Sciences Research Council (BBSRC) [BB/H013180/1, BB/E024203/1]
- Welcome Trust [091163/Z/10/Z]
- Wellcome Trust [091163/Z/10/Z] Funding Source: Wellcome Trust
- Biotechnology and Biological Sciences Research Council [BB/M002969/1, BB/H013180/1, BB/E024203/1] Funding Source: researchfish
- BBSRC [BB/H013180/1, BB/E024203/1, BB/M002969/1] Funding Source: UKRI
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.
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