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Journal article

The aldehyde dehydrogenase, AldA, is essential for L-1,2-propanediol utilization in laboratory-evolved Escherichia coli

From

Cairo University1

University of California at San Diego2

Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark3

New Bioactive Compounds, Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark4

Most Escherichia coli strains are naturally unable to grow on 1,2-propanediol (PDO) as a sole carbon source. Recently, however, a K-12 descendent E. coli strain was evolved to grow on 1,2-PDO, and it was hypothesized that this evolved ability was dependent on the aldehyde dehydrogenase, AldA, which is highly conserved among members of the family Enterobacteriacea.

To test this hypothesis, we first performed computational model simulation, which confirmed the essentiality of the aldA gene for 1,2-PDO utilization by the evolved PDO-degrading E. coli. Next, we deleted the aldA gene from the evolved strain, and this deletion was sufficient to abolish the evolved phenotype.

On re-introducing the gene on a plasmid, the evolved phenotype was restored. These findings provide experimental evidence for the computationally predicted role of AldA in 1,2-PDO utilization, and represent a good example of E. coli robustness, demonstrated by the bacterial deployment of a generalist enzyme (here AldA) in multiple pathways to survive carbon starvation and to grow on a non-native substrate when no native carbon source is available.

Language: English
Year: 2017
Pages: 47-52
ISSN: 16180623 and 09445013
Types: Journal article
DOI: 10.1016/j.micres.2016.10.006
ORCIDs: Charusanti, Pep

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