Building modular hemicellulose synthases, now out in Biotechnology for Biofuels

We are happy to announce the publication of our work on modular hemicellulose production in Biotechnology for Biofuels, a leading (open-access!) journal for advancing the biological production of fuels, chemicals, and biomaterials. Here, we describe how enzymes from the cellulose synthase-like superfamily (found throughout the plant kingdom) can be assembled as modular parts (akin to LEGO bricks) to modulate their function and effects on eukaryotic cell growth.

Fig. 1

Reference:

Robert, M., Waldhauer, J., Stritt, F. et al. Modular biosynthesis of plant hemicellulose and its impact on yeast cells. Biotechnol Biofuels 14, 140 (2021). https://doi.org/10.1186/s13068-021-01985-z

This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. 

Previously the article was available on bioRxiv preprint server: https://doi.org/10.1101/2021.04.20.440611

Update to our bioRxiv preprint

We significantly revised our preprint on the modular biosynthesis of plant heteromannans and uploaded the new version to bioRxiv.

Full-text: https://www.biorxiv.org/content/10.1101/2021.04.20.440611v2.full

Original post

New preprint on yeast bioengineering to produce modular plant hemicellulose

Despite rising interest in the engineering of polysaccharide-based biomaterials, relatively little is known about how plant hemicelluloses can be built and tailored in non-plant cell factories. Pichia pastoris is a promising host to study cellulose synthase-like A (CSLA; heteromannan synthases) and CSLC (xyloglucan synthase) activities but the functions of specific protein motifs and the impact…

February publication update

We are happy to have contributed to a new publication that appeared in Science Advances on the February 10. This study unveils how jasmonate signaling is initiated in the korrigan1 (kor1) cellulose-deficient mutant, and multiple ways in which it can be complemented. The work was lead by Stefan Mielke in Debora Gasperini’s research group at IPB Halle.

Article: https://doi.org/10.1126/sciadv.abf0356

Catalin Voiniciuc performed the cell wall analyses, and would like to acknowledge the valuable technical assistance of Christine Wagner and Bo Yang. The Science Advances study was originally available as a pre-print:

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February also marks the release of a correction to the Voiniciuc et al. (2018) Plant Physiology study of pectin biosynthetic enzymes. Unfortunately, there was an accidental mix-up of GAUT11 and another GAUT protein expressed at the same time. Catalin would like to thank the co-authors for reporting the problem affecting Figure 5 and Supplemental Figure 4A, and repeating the experiments. The corrigendum has addressed this issue and shows that the original results and conclusions that GAUT11 is a galacturonosyltransferase (GalAT) that elongates homogalacturonan (HG) are unaffected.

Original article: https://doi.org/10.1104/pp.18.00584

Corrigendum: https://doi.org/10.1093/plphys/kiaa037

New publication in New Phytologist

Our revised manuscript on the roles of branched xylan and heteromannan (previously available as a preprint) in controlling seed mucilage properties and early growth in salt stress has now been peer-reviewed.

Read the open-access article here: https://doi.org/10.1111/nph.17056

New publication on wheat mannan

A collaborative study of mannan polysaccharide production in wheat (Triticum aestivum) is now published in the journal Plant Science. Wheat-like polymers that normally accumulate in the developing endosperm of the grain were produced in two heterologous hosts by the expression of a single enzyme, TaCSLA12. Additional mannan-related genes were identified in the wheat endosperm but were not essential for making the polysaccharides in yeast. Moreover, a wheat-like mannan production in a glucomannan-deficient Arabidopsis thaliana triple mutant (csla2 csla3 csla9) did not alter the plant morphology.

Congratulations to our colleagues at INRAE (Nantes, France; who led the study), the Joint BioEnergy Institute (Berkeley, California), Rothamsted Research (UK), and Heinrich Heine University (Düsseldorf, Germany; where our experimental work was conducted).

Read more at https://doi.org/10.1016/j.plantsci.2020.110693

Fig. 2 from the study. Subcellular localization of enzymes that may be involved in mannan production. (Source: https://doi.org/10.1016/j.plantsci.2020.110693)

Fig. 3 from the study. Quantification of beta-mannan production in yeast cells after plant enzyme expression. (Source: https://doi.org/10.1016/j.plantsci.2020.110693)