Functional Genomic Study of Exogenous
            <i>n</i>
            -Butanol Stress in
            <i>Escherichia coli</i>

Rutherford, Becky J.; Dahl, Robert H.; Price, Robert M.; Szmidt, Heather L.; Benke, Peter I.; Mukhopadhyay, Aindrila; Keasling, Jay D.

doi:10.1128/aem.02323-09

Cited by 215 publications

(279 citation statements)

References 51 publications

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“…Challenge of E. coli DH1 with n-butanol during mid-log growth transiently activated yqhD; 6-fold induction was observed at 30 minutes, with the 80 and 195 minute samples showing less than a 2-fold change relative to the control sample (Rutherford et al 2010). …”

Section: E Coli Omics Data (University Of Oklahoma Gene Expression Dmentioning

confidence: 98%

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YqhD: a broad-substrate range aldehyde reductase with various applications in production of biorenewable fuels and chemicals

Jarboe

2010

Appl Microbiol Biotechnol

131

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The Escherichia coli NADPH-dependent aldehyde reductase YqhD has contributed to a variety of metabolic engineering projects for production of biorenewable fuels and chemicals. As a scavenger of toxic aldehydes produced by lipid peroxidation, YqhD has reductase activity for a broad range of short-chain aldehydes, including butyraldehyde, glyceraldehyde, malondialdehyde, isobutyraldehyde, methylglyoxal, propanealdehyde, acrolein, furfural, glyoxal, 3-hydroxypropionaldehyde, glycolaldehyde, acetaldehyde, and acetol. This reductase activity has proven useful for the production of biorenewable fuels and chemicals, such as isobutanol and 1,3-and 1,2-propanediol; additional capability exists for production of 1-butanol, 1-propanol, and allyl alcohol. A drawback of this reductase activity is the diversion of valuable NADPH away from biosynthesis. This YqhD-mediated NADPH depletion provides sufficient burden to contribute to growth inhibition by furfural and 5-hydroxymethyl furfural, inhibitory contaminants of biomass hydrolysate. The structure of YqhD has been characterized, with identification of a Zn atom in the active site. Directed engineering efforts have improved utilization of 3-hydroxypropionaldehyde and NADPH. Most recently, two independent projects have demonstrated regulation of yqhD by YqhC, where YqhC appears to function as an aldehyde sensor. AbstractThe Escherichia coli NADPH-dependent aldehyde reductase YqhD has contributed to a variety of metabolic engineering projects for production of biorenewable fuels and chemicals.As a scavenger of toxic aldehydes produced by lipid peroxidation, YqhD has reductase activity for a broad range of short-chain aldehydes, including butyraldehyde, glyceraldehyde, malondialdehyde, isobutyraldehyde, methylglyoxal, propanealdehyde, acrolein, furfural, glyoxal, 3-hydroxypropionaldehyde, glycolaldehyde, acetaldehyde and acetol. This reductase activity has proven useful for the production of biorenewable fuels and chemicals, such as isobutanol and 1,3-and 1,2-propanediol; additional capability exists for production of 1-butanol, 1-propanol and allyl alcohol. A drawback of this reductase activity is the diversion of valuable NADPH away from biosynthesis. This YqhD-mediated NADPH depletion provides sufficient burden to

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Section: E Coli Omics Data (University Of Oklahoma Gene Expression Dmentioning

confidence: 98%

“…Additionally, a BW25113 yqhD deletion mutant showed increased sensitivity to butanol challenge (Rutherford et al 2010). Given that superoxide dismutase sodA was also activated, the authors attributed this yqhD activation to oxidative stress.…”

Section: E Coli Omics Data (University Of Oklahoma Gene Expression Dmentioning

confidence: 99%

YqhD: a broad-substrate range aldehyde reductase with various applications in production of biorenewable fuels and chemicals

Jarboe

2010

Appl Microbiol Biotechnol

131

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“…Downregulation of methionine synthesis genes was also observed in E. coli under butanol stress. 15 As methionine is the first amino acid residue in any protein, E. coli could control the global protein expression by depressing methionine biosynthesis under stress conditions.…”

Section: Proteins Involved In Amino Acids Metabolismmentioning

confidence: 99%

Development of a 3-hydroxypropionate resistantEscherichia colistrain

et al. 2016

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3-hydroxypropionate (3HP) is an important platform chemical, and its biosynthesis is severely restricted by the toxicity of 3HP on cell growth and survival. To improve Escherichia coli resistance to 3HP and reduce the total production cost in industrial applications, we have identified variations in protein expression level exposed to sub-lethal concentration of this chemical using 2-dimensional gel electrophoresis. Under 3HP stress, the amount of 46 proteins was increased while the amount of 23 proteins was reduced. According to the proteomic results, overexpression of some identified proteins significantly increased the E. coli survival rate under 3HP stress. This study shed light on clues for developing E. coli strains with higher resistance to 3HP toxicity and lower production cost for industrial applications.

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“…One of such studies, performed on the natural producer C. butyricum growing on glycerol, proposed that the inhibitory effect of this compound was similar to that produced by other diols, including membrane destabilization (49). Proteomic studies performed in E. coli strains accumulating ethanol and butanol have reported an increase in the content of HSPs (35,50), while the accumulation of 1,3-PDO in C. butyricum was also observed to trigger the synthesis of HSPs in a fashion similar to that observed in solvent-producing bacteria (51). Analysis of the genetic basis for tolerance to biofuels and other chemicals in several bacteria has revealed that it is a complex phenomenon, in which many different aspects and genes are involved, obviously including HSPs (52,53).…”

Section: Discussionmentioning

confidence: 99%

A New Player in the Biorefineries Field: Phasin PhaP Enhances Tolerance to Solvents and Boosts Ethanol and 1,3-Propanediol Synthesis in Escherichia coli

Mezzina

Alvarez

Egoburo

et al. 2017

Appl Environ Microbiol

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The microbial production of biofuels and other added-value chemicals is often limited by the intrinsic toxicity of these compounds. The phasin PhaP from the soil bacterium Azotobacter sp. strain FA8 is a polyhydroxyalkanoate granuleassociated protein that protects recombinant Escherichia coli against several kinds of stress. PhaP enhances growth and poly(3-hydroxybutyrate) synthesis in polymerproducing recombinant strains and reduces the formation of inclusion bodies during overproduction of heterologous proteins. In this work, the heterologous expression of this phasin in E. coli was used as a strategy to increase tolerance to several biotechnologically relevant chemicals. PhaP was observed to enhance bacterial fitness in the presence of biofuels, such as ethanol and butanol, and other chemicals, such as 1,3-propanediol. The effect of PhaP was also studied in a groELS mutant strain, in which both GroELS and PhaP were observed to exert a beneficial effect that varied depending on the chemical tested. Lastly, the potential of PhaP and GroEL to enhance the accumulation of ethanol or 1,3-propanediol was analyzed in recombinant E. coli. Strains that overexpressed either groEL or phaP had increased growth, reflected in a higher final biomass and product titer than the control strain. Taken together, these results add a novel application to the already multifaceted phasin protein group, suggesting that expression of these proteins or other chaperones can be used to improve the production of biofuels and other chemicals.IMPORTANCE This work has both basic and applied aspects. Our results demonstrate that a phasin with chaperone-like properties can increase bacterial tolerance to several biochemicals, providing further evidence of the diverse properties of these proteins. Additionally, both the PhaP phasin and the well-known chaperone GroEL were used to increase the biosynthesis of the biotechnologically relevant compounds ethanol and 1,3-propanediol in recombinant E. coli. These findings open the road for the use of these proteins for the manipulation of bacterial strains to optimize the synthesis of diverse bioproducts from renewable carbon sources.KEYWORDS Escherichia coli, ethanol, butanol, 1,3-propanediol, chaperone, GroEL, PhaP, metabolic engineering F ossil oil, or petroleum, has been utilized by humankind for many centuries, but since the mid-18th century the number and variety of applications for this product have sharply increased, so that nowadays derivatives of this nonrenewable substrate are present in almost every aspect of modern life (1). We use petroleum derivatives as our main source of energy but also as a starting point for the synthesis of many different

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Functional Genomic Study of Exogenous n -Butanol Stress in Escherichia coli

Cited by 215 publications

References 51 publications

YqhD: a broad-substrate range aldehyde reductase with various applications in production of biorenewable fuels and chemicals

YqhD: a broad-substrate range aldehyde reductase with various applications in production of biorenewable fuels and chemicals

Development of a 3-hydroxypropionate resistantEscherichia colistrain

A New Player in the Biorefineries Field: Phasin PhaP Enhances Tolerance to Solvents and Boosts Ethanol and 1,3-Propanediol Synthesis in Escherichia coli

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