Evidence map›Paper›PMID 36153520›Full record

ArticleBMC biology2022

Tuning heterologous glucan biosynthesis in yeast to understand and exploit plant starch diversity.

Barbara Pfister, Jessica M Shields, Tobias Kockmann, Jonas Grossmann, Melanie R Abt, Martha Stadler, Samuel C Zeeman

Open access · goldAbstract read
In one paragraph

Article in BMC biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.5field-weighted citation impact, top 42% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

5 citing papers in PubMed, 7 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 3 institutions in 2 countries.

Barbara PfisterInstitute of Molecular Plant Biology, ETH Zurich, 8092, Zurich, Switzerland. bpfister@ethz.ch.ORCID 0000-0002-4183-9625
Jessica M ShieldsInstitute of Molecular Plant Biology, ETH Zurich, 8092, Zurich, Switzerland.ORCID 0000-0003-4246-9862
Tobias KockmannFunctional Genomics Center Zurich, ETH Zurich, 8057, Zurich, Switzerland.ORCID 0000-0002-1847-885X
Jonas GrossmannFunctional Genomics Center Zurich, ETH Zurich, 8057, Zurich, Switzerland.ORCID 0000-0002-6899-9020
Melanie R AbtInstitute of Molecular Plant Biology, ETH Zurich, 8092, Zurich, Switzerland.ORCID 0000-0002-3347-3969
Martha StadlerInstitute of Molecular Plant Biology, ETH Zurich, 8092, Zurich, Switzerland.ORCID 0000-0003-2402-8852
Samuel C ZeemanInstitute of Molecular Plant Biology, ETH Zurich, 8092, Zurich, Switzerland.ORCID 0000-0002-2791-0915
ETH Zurich · CHSIB Swiss Institute of Bioinformatics · CHUniversity of Exeter · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundStarch, a vital plant-derived polysaccharide comprised of branched glucans, is essential in nutrition and many industrial applications. Starch is often modified post-extraction to alter its structure and enhance its functionality. Targeted metabolic engineering of crops to produce valuable and versatile starches requires knowledge of the relationships between starch biosynthesis, structure, and properties, but systematic studies to obtain this knowledge are difficult to conduct in plants. Here we used Saccharomyces cerevisiae as a testbed to dissect the functions of plant starch biosynthetic enzymes and create diverse starch-like polymers.

resultsWe explored yeast promoters and terminators to tune the expression levels of the starch-biosynthesis machinery from Arabidopsis thaliana. We systematically modulated the expression of each starch synthase (SS) together with a branching enzyme (BE) in yeast. Protein quantification by parallel reaction monitoring (targeted proteomics) revealed unexpected effects of glucan biosynthesis on protein abundances but showed that the anticipated broad range of SS/BE enzyme ratios was maintained during the biosynthetic process. The different SS/BE ratios clearly influenced glucan structure and solubility: The higher the SS/BE ratio, the longer the glucan chains and the more glucans were partitioned into the insoluble fraction. This effect was irrespective of the SS isoform, demonstrating that the elongation/branching ratio controls glucan properties separate from enzyme specificity.

conclusionsOur results provide a quantitative framework for the in silico design of improved starch biosynthetic processes in plants. Our study also exemplifies a workflow for the rational tuning of a complex pathway in yeast, starting from the selection and evaluation of expression modules to multi-gene assembly and targeted protein monitoring during the biosynthetic process.

Indexed as

1,4-alpha-Glucan Branching EnzymeArabidopsisStarch SynthaseGlucansPlantsProtein IsoformsSaccharomyces cerevisiaeStarch1,4-alpha-Glucan Branching EnzymeGlucansProtein IsoformsStarchStarch SynthaseAmylopectin structureArabidopsis thalianaHeterologous expression in yeastParallel reaction monitoring, ProteomicsStarch biosynthesisYFP reporter

Identifiers

PMID36153520
PMCPMC9509603
OpenAlexW4296946231

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.