GroE chaperonins assisted functional expression of bacterial enzymes in <i>Saccharomyces cerevisiae</i>

Xia, Peng‐Fei; Zhang, Guo-Chang; Liu, Jing Jing; Kwak, Suryang; Tsai, Chi‐Chin; Kong, In Iok; Sung, Bong Hyun; Sohn, Jae Hak; Wang, Shu Guang

doi:10.1002/bit.25980

Cited by 27 publications

(29 citation statements)

References 44 publications

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“…Similarly, an unbalanced pathway might lead to accumulation of a toxic intermediate, which can be alleviated by overexpressing a known rate-limiting enzyme [174]. Some compensatory mechanisms are also likely to be broadly-effective, such as chaperone overexpression to improve folding of heterologous proteins [175].…”

Section: Minimizing Interactions With the Host Or Other Pathwaysmentioning

confidence: 99%

Modular Engineering of Biomass Degradation Pathways

Chaves

Presley

2019

Processes

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Production of fuels and chemicals from renewable lignocellulosic feedstocks is a promising alternative to petroleum-derived compounds. Due to the complexity of lignocellulosic feedstocks, microbial conversion of all potential substrates will require substantial metabolic engineering. Non-model microbes offer desirable physiological traits, but also increase the difficulty of heterologous pathway engineering and optimization. The development of modular design principles that allow metabolic pathways to be used in a variety of novel microbes with minimal strain-specific optimization will enable the rapid construction of microbes for commercial production of biofuels and bioproducts. In this review, we discuss variability of lignocellulosic feedstocks, pathways for catabolism of lignocellulose-derived compounds, challenges to heterologous engineering of catabolic pathways, and opportunities to apply modular pathway design. Implementation of these approaches will simplify the process of modifying non-model microbes to convert diverse lignocellulosic feedstocks.

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Section: Minimizing Interactions With the Host Or Other Pathwaysmentioning

confidence: 99%

Modular Engineering of Biomass Degradation Pathways

Chaves

Presley

2019

Processes

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“…A recent study systematically analyzed the GroE dependent proteins in E. coli, and found that 57 proteins could not be active in their native host E. coli without a well-functioning GroE chaperone system [31,32]. Moreover, it has been demonstrated that the E. coli xylose isomerase and arabinose isomerase, both previously reported as being non-functional in yeast [33,34], can work well in S. cerevisiae via co-expression of E. coli GroE [35]. Thus, the chaperone systems can also help with the expression of heterologous enzymes and pathways.…”

Section: Engineering Strain Tolerance Towards Organic Solventsmentioning

confidence: 99%

“…One major contribution comes from our constantly improving DNA reading and writing capabilities, which provide valuable gene resources and promising genetic tools. Nevertheless, not all target genes can be functionally expressed in non-homologous hosts, especially in trans-species and trans-domain cases [35,70]. Proteins must achieve functional conformations to work correctly.…”

Section: Trans-species and -Domains Expression Of Heterologous Proteinsmentioning

confidence: 99%

“…The analog of the bacterial GroE system in yeast is located in mitochondria rather than cytosol, and the cytosolic HSP60 system in yeast is different from the bacterial GroE system regarding substrates and working mechanisms [28]. Therefore, researchers discovered that the mismatching of the chaperonin systems between prokaryotic and eukaryotic cells might be the reason some bacterial enzymes, such as E. coli xylose isomerase and arabinose isomerase, cannot be functionally expressed in yeast [35]. The results showed that functional expression of E. coli xylose isomerase and arabinose isomerase, as well as the Agrobacterium tumefaciens D-psicose epimerase, can be achieved in S. cerevisiae via co-expression the E. coli GroE chaperonins.…”

Section: Improving the Temperature Tolerancementioning

confidence: 99%

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The Role of GroE Chaperonins in Developing Biocatalysts for Biofuel and Chemical Production

Xia¹,

Turner²,

Jayakody³

2016

Enz Eng

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As the need and interest for producing renewable biofuels and biochemical has grown, new avenues to improve product yields and productivity have been explored. Specifically, improving the tolerance of host microbes towards stressors, such as heat shock or the presence of harmful solvents, has been an especially important route to improve industrial-scale chemical production. In this review, we discuss recent advances in microbial engineering for renewable chemical production through the introduction and expression of chaperonins, especially the bacterial GroE complex. The GroE complex provides a closed-off environment and allows vital proteins to enter and engage in post-translational folding or refolding in a more-ideal environment, allowing the microbe to possess increased survival rates in low/high temperatures or in high concentrations of otherwise harmful end-products. Overall, we highlighted how chaperonin systems such as the GroE complex could have many industrially-relevant uses in the coming years.

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“…Recently, the E. coli chaperonins GroEL-GroES complex where co-expressed in S. cerevisiae with xylose isomerase and arabinose isomerase from the same bacteria, which allowed the yeast cells to grow in xylose and arabinose as carbon sources [ 13 ]. Expression of the enzymes from E. coli without the chaperonins was unable to achieve this effect, which indicates an important role of this complex in enzyme activity.…”

Section: Introductionmentioning

confidence: 99%

Conversion of an inactive xylose isomerase into a functional enzyme by co-expression of GroEL-GroES chaperonins in Saccharomyces cerevisiae

et al. 2017

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BackgroundSecond-generation ethanol production is a clean bioenergy source with potential to mitigate fossil fuel emissions. The engineering of Saccharomyces cerevisiae for xylose utilization is an essential step towards the production of this biofuel. Though xylose isomerase (XI) is the key enzyme for xylose conversion, almost half of the XI genes are not functional when expressed in S. cerevisiae. To date, protein misfolding is the most plausible hypothesis to explain this phenomenon.ResultsThis study demonstrated that XI from the bacterium Propionibacterium acidipropionici becomes functional in S. cerevisiae when co-expressed with GroEL-GroES chaperonin complex from Escherichia coli. The developed strain BTY34, harboring the chaperonin complex, is able to efficiently convert xylose to ethanol with a yield of 0.44 g ethanol/g xylose. Furthermore, the BTY34 strain presents a xylose consumption rate similar to those observed for strains carrying the widely used XI from the fungus Orpinomyces sp. In addition, the tetrameric XI structure from P. acidipropionici showed an elevated number of hydrophobic amino acid residues on the surface of protein when compared to XI commonly expressed in S. cerevisiae.ConclusionsBased on our results, we elaborate an extensive discussion concerning the uncertainties that surround heterologous expression of xylose isomerases in S. cerevisiae. Probably, a correct folding promoted by GroEL-GroES could solve some issues regarding a limited or absent XI activity in S. cerevisiae. The strains developed in this work have promising industrial characteristics, and the designed strategy could be an interesting approach to overcome the non-functionality of bacterial protein expression in yeasts.Electronic supplementary materialThe online version of this article (10.1186/s12896-017-0389-7) contains supplementary material, which is available to authorized users.

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GroE chaperonins assisted functional expression of bacterial enzymes in Saccharomyces cerevisiae

Cited by 27 publications

References 44 publications

Modular Engineering of Biomass Degradation Pathways

Modular Engineering of Biomass Degradation Pathways

The Role of GroE Chaperonins in Developing Biocatalysts for Biofuel and Chemical Production

Conversion of an inactive xylose isomerase into a functional enzyme by co-expression of GroEL-GroES chaperonins in Saccharomyces cerevisiae

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