Complementing the intrinsic repertoire of Ustilago maydis for degradation of the pectin backbone polygalacturonic acid

Stoffels, Peter; Müller, Markus Jan; Stachurski, Sarah; Terfrüchte, Marius; Schröder, Sebastian; Ihling, Nina; Wierckx, Nick; Feldbrügge, Michael; Schipper, Kerstin; Büchs, Jochen

doi:10.1016/j.jbiotec.2019.10.022

Cited by 23 publications

(14 citation statements)

References 78 publications

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“…Here, we use Cts1 as a carrier for valuable heterologous proteins. Exploiting the unconventional secretion route brings the advantage that N- glycosylation is circumvented and thus, sensitive proteins like bacterial enzymes can be exported in an active state ( Sarkari et al, 2014 ; Terfrüchte et al, 2017 ; Stoffels et al, 2019 ). The screen will be adapted to select for mutants with enhanced marker secretion to eliminate existing bottlenecks and thus enhance yields ( Terfrüchte et al, 2018 ).…”

Section: Discussionmentioning

confidence: 99%

A Novel Factor Essential for Unconventional Secretion of Chitinase Cts1

et al. 2020

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Subcellular targeting of proteins is essential to orchestrate cytokinesis in eukaryotic cells. During cell division of Ustilago maydis , for example, chitinases must be specifically targeted to the fragmentation zone at the site of cell division to degrade remnant chitin and thus separate mother and daughter cells. Chitinase Cts1 is exported to this location via an unconventional secretion pathway putatively operating in a lock-type manner. The underlying mechanism is largely unexplored. Here, we applied a forward genetic screen based on UV mutagenesis to identify components essential for Cts1 export. The screen revealed a novel factor termed Jps1 lacking known protein domains. Deletion of the corresponding gene confirmed its essential role for Cts1 secretion. Localization studies demonstrated that Jps1 colocalizes with Cts1 in the fragmentation zone of dividing yeast cells. While loss of Jps1 leads to exclusion of Cts1 from the fragmentation zone and strongly reduced unconventional secretion, deletion of the chitinase does not disturb Jps1 localization. Yeast-two hybrid experiments indicate that the two proteins might interact. In essence, we identified a novel component of unconventional secretion that functions in the fragmentation zone to enable export of Cts1. We hypothesize that Jps1 acts as an anchoring factor for Cts1.

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Section: Discussionmentioning

confidence: 99%

A Novel Factor Essential for Unconventional Secretion of Chitinase Cts1

et al. 2020

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“…Finally, the fusion of FPP synthase (FPPS) and germacrene A synthase (GAS) has been shown to increase sesquiterpenoid yield, as FPP was directly funneled into product formation (Hu et al, 2017). Furthermore, in combination with the enhanced biomass degrading ability of U. maydis for use of alternative carbon sources (Geiser et al, 2016b;Stoffels et al, 2020), we envision to generate a sustainable consolidated bioprocessing strategy for next generation bioengineering of terpenoid production.…”

Section: Resultsmentioning

confidence: 99%

“…At present, U. maydis strains are being optimized to convert plant biomass into valuable products. Strains have been successfully engineered to grow on cellulose, xylose, and polygalacturonic acid (Geiser et al, 2016a;Stoffels et al, 2020). The latter is a major component of pectin.…”

Section: Introductionmentioning

confidence: 99%

Ustilago maydis Serves as a Novel Production Host for the Synthesis of Plant and Fungal Sesquiterpenoids

et al. 2020

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Sesquiterpenoids are important secondary metabolites with various pharma-and nutraceutical properties. In particular, higher basidiomycetes possess a versatile biosynthetic repertoire for these bioactive compounds. To date, only a few microbial production systems for fungal sesquiterpenoids have been established. Here, we introduce Ustilago maydis as a novel production host. This model fungus is a close relative of higher basidiomycetes. It offers the advantage of metabolic compatibility and potential tolerance for substances toxic to other microorganisms. We successfully implemented a heterologous pathway to produce the carotenoid lycopene that served as a straightforward read-out for precursor pathway engineering. Overexpressing genes encoding enzymes of the mevalonate pathway resulted in increased lycopene levels. Verifying the subcellular localization of the relevant enzymes revealed that initial metabolic reactions might take place in peroxisomes: despite the absence of a canonical peroxisomal targeting sequence, acetyl-CoA C-acetyltransferase Aat1 localized to peroxisomes. By expressing the plant (+)-valencene synthase CnVS and the basidiomycete sesquiterpenoid synthase Cop6, we succeeded in producing (+)valencene and α-cuprenene, respectively. Importantly, the fungal compound yielded about tenfold higher titers in comparison to the plant substance. This proof of principle demonstrates that U. maydis can serve as promising novel chassis for the production of terpenoids.

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“…Pectins, together with hemicelluloses and proteins, form the base matrix of the middle plate and cell walls ( Stoffels et al, 2020 ). Most of the pectin consists of alpha- d -galacturonic acid.…”

Section: Introductionmentioning

confidence: 99%

An overview of biomass conversion: exploring new opportunities

Fülöp¹,

Ecker²

2020

PeerJ

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Recycling biomass is indispensable these days not only because fossil energy sources are gradually depleted, but also because pollution of the environment, caused by the increasing use of energy, must be reduced. This article intends to overview the results of plant biomass processing methods that are currently in use. Our aim was also to review published methods that are not currently in use. It is intended to explore the possibilities of new methods and enzymes to be used in biomass recycling. The results of this overview are perplexing in almost every area. Advances have been made in the pre-treatment of biomass and in the diversity and applications of the enzymes utilized. Based on molecular modeling, very little progress has been made in the modification of existing enzymes for altered function and adaptation for the environmental conditions during the processing of biomass. There are hardly any publications in which molecular modeling techniques are used to improve enzyme function and to adapt enzymes to various environmental conditions. Our view is that using modern computational, biochemical, and biotechnological methods would enable the purposeful design of enzymes that are more efficient and suitable for biomass processing.

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Complementing the intrinsic repertoire of Ustilago maydis for degradation of the pectin backbone polygalacturonic acid

Cited by 23 publications

References 78 publications

A Novel Factor Essential for Unconventional Secretion of Chitinase Cts1

A Novel Factor Essential for Unconventional Secretion of Chitinase Cts1

Ustilago maydis Serves as a Novel Production Host for the Synthesis of Plant and Fungal Sesquiterpenoids

An overview of biomass conversion: exploring new opportunities

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