FadD Is Required for Utilization of Endogenous Fatty Acids Released from Membrane Lipids

Pech-Canul, Ángel de la Cruz; Nogales, Joaquina; Miranda-Molina, Alfonso; Álvarez, Laura; Geiger, Otto; Soto, Marı́a José; López‐Lara, Isabel M.

doi:10.1128/jb.05450-11

Cited by 64 publications

(69 citation statements)

References 51 publications

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“…The results obtained from the fadD deletion mutant, however, do not deny the existing LCFA transport mechanism that a LCFA molecule must be abstracted from the inner membrane by FadD to get into cytoplasm. The lipid composition in fadD deletion mutants is known to be different from the wildtype strain (Pech-Canul et al 2011), and there have not been any studies on whether the membrane structure is reasonably conserved when fadD is deleted. Therefore, experimental data with the fadD deletion mutant in this study cannot conclusively infer the detailed transport mechanism of the wild-type strain.…”

Section: Discussionmentioning

confidence: 98%

fadD deletion and fadL overexpression in Escherichia coli increase hydroxy long-chain fatty acid productivity

Bae

Park

Jung

et al. 2014

Appl Microbiol Biotechnol

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A major problem of long-chain fatty acid (LCFA) hydroxylation using Escherichia coli is that FadD (long-chain fatty acyl-CoA synthetase), which is necessary for exogenous LCFA transport, also initiates cellular consumption of LCFA. In this study, an effective method to prevent the cellular consumption of LCFA without impairing its transport is proposed. The main idea is that a heterologous enzyme which consumes LCFA can replace FadD in LCFA transport. For the model heterologous enzyme, CYP153A from Marinobacter aquaeolei, which converts palmitic acid into ω-hydroxy palmitic acid, was expressed in E. coli. When fadD was deleted from an E. coli strain, CYP153A indeed maintained the ability to transport LCFA. A disadvantage of fadD deletion mutant is the fact that FadD deficiency downregulates the transcription of fadL (outer membrane LCFA transporter) via FadR (fatty acid metabolism regulator protein), was solved by fadL overexpression from a plasmid. In addition, the overexpression of fadL was able to offset catabolite repression on fadL, allowing glucose to be used as the primary carbon source. In conclusion, the strain with fadD deletion and fadL overexpression showed 5.5-fold increase in productivity compared to the wild-type strain, converting 2.6 g/L (10.0 mM) of palmitic acid into 2.4 g/L (8.8 mM) of ω-hydroxy palmitic acid in a shake flask. This simple genetic manipulation can be applied to any LCFA hydroxylation using E. coli.

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Section: Discussionmentioning

confidence: 98%

fadD deletion and fadL overexpression in Escherichia coli increase hydroxy long-chain fatty acid productivity

Bae

Park

Jung

et al. 2014

Appl Microbiol Biotechnol

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“…Indeed, it has been reported that members of the FadR regulon might be activated in stationary phase (20,67), and several fad genes have been reported to be upregulated during the stringent response (34). A recent report suggested that free fatty acids might accompany envelope remodeling during stationary phase (68), which might explain derepression of the fad genes. The reduced amount of FadR protein in stationary phase observed in our study, coupled with the increase in ppGpp concentration that occurs upon entry into stationary phase (63) and the resulting effects on FadR synthesis, might also contribute to effects on the FadR regulon (Fig.…”

Section: Discussionmentioning

confidence: 99%

Transcription of the Escherichia coli Fatty Acid Synthesis OperonfabHDGIs Directly Activated by FadR and Inhibited by ppGpp

Rekoske

Lemke

et al. 2013

J Bacteriol

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bIn Escherichia coli, FadR and FabR are transcriptional regulators that control the expression of fatty acid degradation and unsaturated fatty acid synthesis genes, depending on the availability of fatty acids. In this report, we focus on the dual transcriptional regulator FadR. In the absence of fatty acids, FadR represses the transcription of fad genes required for fatty acid degradation. However, FadR is also an activator, stimulating transcription of the products of the fabA and fabB genes responsible for unsaturated fatty acid synthesis. In this study, we show that FadR directly activates another fatty acid synthesis promoter, PfabH, which transcribes the fabHDG operon, indicating that FadR is a global regulator of both fatty acid degradation and fatty acid synthesis. We also demonstrate that ppGpp and its cofactor DksA, known primarily for their role in regulation of the synthesis of the translational machinery, directly inhibit transcription from the fabH promoter. ppGpp also inhibits the fadR promoter, thereby reducing transcription activation of fabH by FadR indirectly. Our study shows that both ppGpp and FadR have direct roles in the control of fatty acid promoters, linking expression in response to both translation activity and fatty acid availability.

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“…The E. coli homolog FadL Ec is required for uptake of exogenous oleic and palmitic acids, but not for reutilization of membrane lipids (5,29). Thus, LCFA uptake through FadL likely is crucial only for utilization of exogenous fatty acids.…”

Section: Discussionmentioning

confidence: 99%

Rhizobial homologs of the fatty acid transporter FadL facilitate perception of long-chain acyl-homoserine lactone signals

Krol

Becker

2014

Proc. Natl. Acad. Sci. U.S.A.

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Significance Bacterial intercellular communication is crucial for developing population and community structures and for pathogenic and symbiotic interactions with eukaryotic hosts. Many Gram-negative bacteria use N-acyl-homoserine lactones (AHLs) in quorum sensing-related signaling. Although it is likely that specific transport mechanisms are required for long-chain AHLs to overcome the outer membrane, mechanisms promoting uptake have not been reported so far. Here we present evidence that homologs of the outer membrane long-chain fatty acid transporter FadL facilitate uptake of long-chain AHLs, which closes an important gap in our understanding of quorum sensing signaling. Our findings suggest that bacteria responding to long-chain AHLs have evolved specificity of FadL toward these signal molecules and have partly lost the ability to transport long-chain fatty acid by this protein.

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FadD Is Required for Utilization of Endogenous Fatty Acids Released from Membrane Lipids

Cited by 64 publications

References 51 publications

fadD deletion and fadL overexpression in Escherichia coli increase hydroxy long-chain fatty acid productivity

fadD deletion and fadL overexpression in Escherichia coli increase hydroxy long-chain fatty acid productivity

Transcription of the Escherichia coli Fatty Acid Synthesis OperonfabHDGIs Directly Activated by FadR and Inhibited by ppGpp

Rhizobial homologs of the fatty acid transporter FadL facilitate perception of long-chain acyl-homoserine lactone signals

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