Abstract
Solvents toxicity is a major limiting factor hampering the cost-effective biotechnological production of chemicals. In Clostridium acetobutylicum, a functionally unknown protein (encoded by SMB_G1518) with a hypothetical alcohol interacting domain was identified. Disruption of SMB_G1518 and/or its downstream gene SMB_G1519 resulted in increased butanol tolerance, while overexpression of SMB_G1518-1519 decreased butanol tolerance. In addition, SMB_G1518-1519 also influences the production of pyruvate:ferredoxin oxidoreductase (PFOR) and flagellar protein hag, the maintenance of cell motility. We conclude that the system of SMB_G1518-1519 protein plays a role in the butanol sensitivity/tolerance phenotype of C. acetobutylicum, and can be considered as potential targets for engineering alcohol tolerance.
Highlights
The toxicity of organic solvents to microorganisms is a major limiting factor hampering the cost-effective biotechnological production of solvents [1,2]
Rationale As alcohol interacting regions are highly conserved in animal cells (Figure S1) and these cysteine-rich zinc finger domains were found in many sequenced microbes, we propose that a protein containing this conserved region might function in modulating butanol tolerance in C. acetobutylicum
protein kinase C (PKC) superfamily contains 8 types of isomers, the mechanism for PKC isomers a and d interacting with anesthetics has been extensively studied [8,9,20]
Summary
The toxicity of organic solvents to microorganisms is a major limiting factor hampering the cost-effective biotechnological production of solvents [1,2]. The concentration of alcohol used clinically might be too low to induce the perturbation of cell membrane in animal cells [7]. Another theory proposes that protein kinase C (PKC) mediates alcohol toxicity. Alcohol binding sites are discretely presented within C1A and C1B, and two of these binding sites were located in the vicinity of the phorbol binding loops, suggesting the modulating function of alcohol [5,8,9] In this way, zinc finger domain plays a vital role in mediating the effects of alcohol on animal cell
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