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Reassessing <i>Escherichia coli</i> as a cell factory for biofuel production
Wang, Chonglong,Pfleger, Brian F,Kim, Seon-Won Elsevier 2017 Current opinion in biotechnology Vol.45 No.-
<P>Via metabolic engineering, industrial microorganisms have the potential to convert renewable substrates into a wide range of biofuels that can address energy security and environmental challenges associated with current fossil fuels. The user-friendly bacterium, <I>Escherichia coli</I>, remains one of the most frequently used hosts for demonstrating production of biofuel candidates including alcohol-, fatty acid- and terpenoid-based biofuels. In this review, we summarize the metabolic pathways for synthesis of these biofuels and assess enabling technologies that assist in regulating biofuel synthesis pathways and rapidly assembling novel <I>E. coli</I> strains. These advances maintain <I>E. coli</I>’s position as a prominent host for developing cell factories for biofuel production.</P> <P><B>Highlights</B></P> <P> <UL> <LI> Biofuel production has been achieved in <I>Escherichia coli</I> by construction of several metabolic pathways. </LI> <LI> The emerging technologies shows great potential in pathway engineering and stain manipulation. </LI> <LI> Tolerance engineering was required to construct an ideal biofuel producing <I>E. coli</I> host. </LI> </UL> </P>
Wang, Chonglong,Park, Ju‐,Eon,Choi, Eui‐,Sung,Kim, Seon‐,Won WILEY‐VCH Verlag 2016 BIOTECHNOLOGY JOURNAL Vol.11 No.10
<P><B>Abstract</B></P><P>Farnesol is a sesquiterpenoid alcohol that has important industrial and medical potential. It is usually synthesized from farnesyl diphosphate (FPP) by farnesol synthase in plants. FPP accumulation can cause up‐regulation of phosphatases capable of FPP hydrolysis, resulting in farnesol production in <I>Escherichia coli</I>. We found that PgpB and YbjG, two integral membrane phosphatases, can hydrolyze FPP into farnesol. Overexpression of FPP synthase (IspA) and PgpB, along with a heterologous mevalonate pathway, enabled recombinant <I>E. coli</I> to produce 526.1 mg/L of farnesol. This result indicates that the phosphatases PgpB and YbjG can be used to construct a novel farnesol synthesis pathway for mass production in <I>E. coli</I>.</P>
Farnesol production from <i>Escherichia coli</i> by harnessing the exogenous mevalonate pathway
Wang, Chonglong,Yoon, Sang‐,Hwal,Shah, Asad Ali,Chung, Young‐,Ryun,Kim, Jae‐,Yean,Choi, Eui‐,Sung,Keasling, Jay D.,Kim, Seon‐,Won Wiley Subscription Services, Inc., A Wiley Company 2010 Biotechnology and bioengineering Vol.107 No.3
<P><B>Abstract</B></P><P>Farnesol (FOH) production has been carried out in metabolically engineered <I>Escherichia coli</I>. FOH is formed through the depyrophosphorylation of farnesyl pyrophosphate (FPP), which is synthesized from isopentenyl pyrophosphate (IPP) and dimethylallyl pyrophosphate (DMAPP) by FPP synthase. In order to increase FPP synthesis, <I>E. coli</I> was metabolically engineered to overexpress <I>ispA</I> and to utilize the foreign mevalonate (MVA) pathway for the efficient synthesis of IPP and DMAPP. Two‐phase culture using a decane overlay of the culture broth was applied to reduce volatile loss of FOH produced during culture and to extract FOH from the culture broth. A FOH production of 135.5 mg/L was obtained from the recombinant <I>E. coli</I> harboring the pTispA and pSNA plasmids for <I>ispA</I> overexpression and MVA pathway utilization, respectively. It is interesting to observe that a large amount of FOH could be produced from <I>E. coli</I> without FOH synthase by the augmentation of FPP synthesis. Introduction of the exogenous MVA pathway enabled the dramatic production of FOH by <I>E. coli</I> while no detectable FOH production was observed in the endogenous MEP pathway‐only control. Biotechnol. Bioeng. 2010;107: 421–429. © 2010 Wiley Periodicals, Inc.</P>
Wang, Chonglong,Zada, Bakht,Wei, Gongyuan,Kim, Seon-Won Elsevier 2017 Bioresource technology Vol.241 No.-
<P><B>Abstract</B></P> <P>Isoprenoids comprise the largest family of natural organic compounds with many useful applications in the pharmaceutical, nutraceutical, and industrial fields. Rapid developments in metabolic engineering and synthetic biology have facilitated the engineering of isoprenoid biosynthetic pathways in <I>Escherichia coli</I> to induce high levels of production of many different isoprenoids. In this review, the stem pathways for synthesizing isoprene units as well as the branch pathways deriving diverse isoprenoids from the isoprene units have been summarized. The review also highlights the metabolic engineering efforts made for the biosynthesis of hemiterpenoids, monoterpenoids, sesquiterpenoids, diterpenoids, carotenoids, retinoids, and coenzyme Q<SUB>10</SUB> in <I>E</I>. <I>coli</I>. Perspectives and future directions for the synthesis of novel isoprenoids, decoration of isoprenoids using cytochrome P450 enzymes, and secretion or storage of isoprenoids in <I>E</I>. <I>coli</I> have also been included.</P> <P><B>Highlights</B></P> <P> <UL> <LI> This review covered production of isoprenoid in <I>E</I>. <I>coli</I> over decades. </LI> <LI> This review summarized progresses of pathway engineering for isoprenoid production. </LI> <LI> This review suggested three directions for isoprenoid production in the future. </LI> </UL> </P>
Ding, Yueyun,Qian, Li,Wang, Li,Wu, Chaodong,Li, DengTao,Zhang, Xiaodong,Yin, Zongjun,Wang, Yuanlang,Zhang, Wei,Wu, Xudong,Ding, Jian,Yang, Min,Zhang, Liang,Shang, Jinnan,Wang, Chonglong,Gao, Yafei Asian Australasian Association of Animal Productio 2020 Animal Bioscience Vol.33 No.2
Objective: Considering the physiological and clinical importance of leptin receptor (LEPR) in regulating obesity and the fact that porcine LEPR expression is not known to be controlled by lncRNAs and miRNAs, we aim to characterize this gene as a potential target of SSC-miR-323 and the lncRNA TCONS_00010987. Methods: Bioinformatics analyses revealed that lncRNA TCONS_00010987 and LEPR have SSC-miR-323-binding sites and that LEPR might be a target of lncRNA TCONS_00010987 based on cis prediction. Wild-type and mutant TCONS_00010987-target sequence fragments and wild-type and mutant LEPR 3'-UTR fragments were generated and cloned into pmiRRB-REPORT<sup>TM</sup>-Control vectors to construct respective recombinant plasmids. HEK293T cells were co-transfected with the SSC-miR-323 mimics or a negative control with constructs harboring the corresponding binding sites and relative luciferase activities were determined. Tissue expression patterns of lncRNA TCONS_00010987, SSC-miR-323, and LEPR in Anqing six-end-white (AQ, the obese breed) and Large White (LW, the lean breed) pigs were detected by real-time quantitative polymerase chain reaction; backfat expression of LEPR protein was detected by western blotting. Results: Target gene fragments were successfully cloned, and the four recombinant vectors were constructed. Compared to the negative control, SSC-miR-323 mimics significantly inhibited luciferase activity from the wild-type TCONS_00010987-target sequence and wild-type LEPR-3'-UTR (p<0.01 for both) but not from the mutant TCONS_00010987-target sequence and mutant LEPR-3'-UTR (p>0.05 for both). Backfat expression levels of TCONS_00010987 and LEPR in AQ pigs were significantly higher than those in LW pigs (p<0.01), whereas levels of SSC-miR-323 in AQ pigs were significantly lower than those in LW pigs (p<0.05). LEPR protein levels in the backfat tissues of AQ pigs were markedly higher than those in LW pigs (p<0.01). Conclusion: LEPR is a potential target of SSC-miR-323, and TCONS_00010987 might act as a sponge for SSC-miR-323 to regulate LEPR expression.
Liu, Yang,Wang, Chonglong,Liu, Zhengzhu,Xu, Jingen,Fu, Weixuan,Wang, Wenwen,Ding, Xiangdong,Liu, Jianfeng,Zhang, Qin Asian Australasian Association of Animal Productio 2012 Animal Bioscience Vol.25 No.8
Neonatal Fc receptor (FcRn) gene encodes a receptor that binds the Fc region of monomeric immunoglobulin G (IgG) and is responsible for IgG transport and stabilization. In this report, the 8,900 bp porcine FcRn genomic DNA structure was identified and putative FcRn protein included 356 amino acids. Alignment and phylogenetic analysis of the porcine FcRn amino acid sequences with their homologies of other species showed high identity. Tissues expression of FcRn mRNA was detected by real time quantitative polymerase chain reaction (Q-PCR), the results revealed FcRn expressed widely in ten analyzed tissues. One single nucleotide polymorphism (SNP) (HQ026019:g.8526 C>T) in exon6 region of porcine FcRn gene was demonstrated by DNA sequencing analysis. A further analysis of SNP genotypes associated with serum Classical Swine Fever Virus antibody (anti-CSFV) concentration was performed in three pig populations including Large White, Landrace and Songliao Black pig (a Chinese indigenous breed). Our results of statistical analysis showed that the SNP had a highly significant association with the level of anti-CSFV antibody (At d 20; At d 35) in serum (p = 0.008; p = 0.0001). Investigation of expression and polymorphisms of the porcine FcRn gene will help us in further understanding the molecular basis of the antibody regulation pathway in the porcine immune response. All these results indicate that FcRn gene might be regarded as a molecular marker for genetic selection of anti-CSFV antibody level in pig disease resistance breeding programmes.