High versus low level expression of the lycopene biosynthesis genes from Pantoea ananatis in Escherichia coli

Albermann, Christoph

doi:10.1007/s10529-010-0422-6

Cited by 19 publications

(13 citation statements)

References 24 publications

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“…Unexpectedly, the carotenoids 3,4,3=,4=-tetradehydrolycopene and 3,4-didehydrolycopene were detected in the homologous complementation PAI ϩ CrtE PAG ϩ CrtB PAG and the heterologous complementation CGI ϩ CrtE PAG ϩ CrtB PAG , respectively. In other studies, the rare, fully saturated 3,4,3=,4=-tetradehydrolycopene was produced when a CrtI generated by directed evolution was involved (18) or wild-type CrtI of P. ananatis was expressed at high levels (11). BLI, CGI, and RBI, which belong to an outgroup of the phylogenetic tree, produced a far smaller amount of carotenoids, suggesting that these heterologous complementations were less efficient in converting phytoene into lycopene.…”

Section: Resultsmentioning

confidence: 89%

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Heterologous Carotenoid-Biosynthetic Enzymes: Functional Complementation and Effects on Carotenoid Profiles in Escherichia coli

Song

Kim

Choi

et al. 2013

Appl Environ Microbiol

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bA limited number of carotenoid pathway genes from microbial sources have been studied for analyzing the pathway complementation in the heterologous host Escherichia coli. In order to systematically investigate the functionality of carotenoid pathway enzymes in E. coli, the pathway genes of carotenogenic microorganisms (Brevibacterium linens, Corynebacterium glutamicum, Rhodobacter sphaeroides, Rhodobacter capsulatus, Rhodopirellula baltica, and Pantoea ananatis) were modified to form synthetic expression modules and then were complemented with Pantoea agglomerans pathway enzymes (CrtE, CrtB, CrtI, CrtY, and CrtZ). The carotenogenic pathway enzymes in the synthetic modules showed unusual activities when complemented with E. coli. For example, the expression of heterologous CrtEs of B. linens, C. glutamicum, and R. baltica influenced P. agglomerans CrtI to convert its substrate phytoene into a rare product-3,4,3=,4=-tetradehydrolycopene-along with lycopene, which was an expected product, indicating that CrtE, the first enzyme in the carotenoid biosynthesis pathway, can influence carotenoid profiles. In addition, CrtIs of R. sphaeroides and R. capsulatus converted phytoene into an unusual lycopene as well as into neurosporene. Thus, this study shows that the functional complementation of pathway enzymes from different sources is a useful methodology for diversifying biosynthesis as nature does.

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Section: Resultsmentioning

confidence: 89%

“…1). The carotenoid biosynthetic pathways of Pantoea have been successfully used as basic pathways for many carotenoid studies (11)(12)(13). The pathway enzymes from different sources have occasionally shown unusual activities or substrate affinities in a heterologous host (14)(15)(16).…”

mentioning

confidence: 99%

Heterologous Carotenoid-Biosynthetic Enzymes: Functional Complementation and Effects on Carotenoid Profiles in Escherichia coli

Song

Kim

Choi

et al. 2013

Appl Environ Microbiol

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“…When high ratio of enzyme to substrate was applied, three‐ and four‐step desaturases from Rvi. gelatinosus favor four‐step desaturation (Stickforth & Sandmann, ), and the four‐step desaturase from P. ananatis could catalyze six‐step desaturation (Albermann, ). The high enzyme concentrations and low substrate concentrations favored further sequential desaturation.…”

Section: Resultsmentioning

confidence: 99%

“…gelatinosus and P. ananatis could even catalyze six-step desaturation to produce 3,4,3′,4′-tetradehydrolycopene when the phytoene supply was insufficient, whereas CrtI catalyzed both three-and four-step desaturations to produce neurosporene and lycopene in Rvi. gelatinosus and catalyzed four-step desaturation to produce lycopene in P. ananatis (Linden et al, 1991;Harada et al, 2001;Albermann, 2011).…”

Section: In Vivo and In Vitro Desaturation Activity Of Crtimentioning

confidence: 99%

Carotenogenesis gene cluster and phytoene desaturase catalyzing both three- and four-step desaturations from Rhodobacter azotoformans

Zhang

Yin

et al. 2012

FEMS Microbiol Lett

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A carotenogenesis gene cluster from the purple nonsulfur photosynthetic bacterium Rhodobacter azotoformans CGMCC 6086 was cloned. A total of eight carotenogenesis genes ( crtA , crtI , crtB , tspO , crtC , crtD , crtE , and crtF ) were located in two separate regions within the genome, a 4.9 kb region containing four clustered genes of crtAIB - tspO and a 5.3 kb region containing four clustered genes of crtCDEF . The organization was unusual for a carotenogenesis gene cluster in purple photosynthetic bacteria. A gene encoding phytoene desaturase ( CrtI ) from Rba. azotoformans was expressed in Escherichia coli. The recombinant CrtI could catalyze both three- and four-step desaturations of phytoene to produce neurosporene and lycopene, and the relative contents of neurosporene and lycopene formed by CrtI were approximately 23% and 75%, respectively. Even small amounts of five-step desaturated 3,4-didehydrolycopene could be produced by CrtI . This product pattern was novel because CrtI produced only neurosporene leading to spheroidene pathway in the cells of Rba. azotoformans. In the in vitro reaction, the relative content of lycopene in desaturated products increased from 19.6% to 62.5% when phytoene reduced from 2.6 to 0.13 μM. The results revealed that the product pattern of CrtI might be affected by the kinetics.

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“…Zhang et al (2014) engineered the E. coli by harbouring IspA/SabS1 or GPPS2/SabS1, the recombinant bacteria could produce the sabinene at the concentration of 0Á96 and 2Á07 mg l À1 respectively. In the same way, carotenoid, lycopene and the other isoprenoids could be produced in the E. coli (Yuan et al 2006;Ajikumar et al 2010;Leonard et al 2010;Wang et al 2010;Albermann 2011). Glyceraldehyde Overexpression of key enzymes in the methylerythritol 4-phosphate pathway…”

Section: Introductionmentioning

confidence: 96%

Strategies of isoprenoids production in engineered bacteria

Wang

2016

J Appl Microbiol

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Summary Isoprenoids are the largest family of natural products, over 40 000 compounds have been described, which have been widely used in various fields. Currently, the isoprenoid products are mainly produced by natural extraction or chemical synthesis, however, limited yield and high cost is far behind the increasing need. Most bacteria synthesize the precursors of isoprenoids through the methylerythritol 4‐phosphate pathway, microbial synthesis of isoprenoids by fermentation becomes more attractive mainly in terms of environmental concern and renewable resources. In this review, the strategies of isoprenoid production in bacteria by synthetic biology are discussed. Introducing foreign genes associated with desired products made it possible to produce isoprenoids in bacteria. Furthermore, the yield of isoprenoids is increased by the strategies of overexpression of native or foreign genes, introducing heterologous mevalonate pathway, balancing of the precursors and inactivating the competing pathway, these methods were used separately or simultaneously.

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High versus low level expression of the lycopene biosynthesis genes from Pantoea ananatis in Escherichia coli

Cited by 19 publications

References 24 publications

Heterologous Carotenoid-Biosynthetic Enzymes: Functional Complementation and Effects on Carotenoid Profiles in Escherichia coli

Heterologous Carotenoid-Biosynthetic Enzymes: Functional Complementation and Effects on Carotenoid Profiles in Escherichia coli

Carotenogenesis gene cluster and phytoene desaturase catalyzing both three- and four-step desaturations from Rhodobacter azotoformans

Strategies of isoprenoids production in engineered bacteria

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