Evidence map›Paper›PMID 25014622›Full record

ArticlePloS one2014

Analysis of the functional interaction of Arabidopsis starch synthase and branching enzyme isoforms reveals that the cooperative action of SSI and BEs results in glucans with polymodal chain length distribution similar to amylopectin.

Henrike Brust, Tanja Lehmann, Christophe D'Hulst, Joerg Fettke

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
4.7field-weighted citation impact, top 5% 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

16 citing papers in PubMed, 44 citations in OpenAlex.

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  15. Formation of starch in plant cells.Cellular and molecular life sciences : CMLS · 2016
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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

4 authors at 2 institutions in 2 countries.

Henrike BrustInstitute of Biochemistry and Biology, University of Potsdam, Potsdam-Golm, Germany.
Tanja LehmannInstitute of Biochemistry and Biology, University of Potsdam, Potsdam-Golm, Germany.
Christophe D'HulstUnité de Glycobiologie Structurale et Fonctionnelle, Université Lille1, Villeneuve d'Ascq, France.
Joerg FettkeInstitute of Biochemistry and Biology, University of Potsdam, Potsdam-Golm, Germany.
University of Potsdam · DEUnité de Glycobiologie Structurale et Fonctionnelle · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Starch synthase (SS) and branching enzyme (BE) establish the two glycosidic linkages existing in starch. Both enzymes exist as several isoforms. Enzymes derived from several species were studied extensively both in vivo and in vitro over the last years, however, analyses of a functional interaction of SS and BE isoforms are missing so far. Here, we present data from in vitro studies including both interaction of leaf derived and heterologously expressed SS and BE isoforms. We found that SSI activity in native PAGE without addition of glucans was dependent on at least one of the two BE isoforms active in Arabidopsis leaves. This interaction is most likely not based on a physical association of the enzymes, as demonstrated by immunodetection and native PAGE mobility analysis of SSI, BE2, and BE3. The glucans formed by the action of SSI/BEs were analysed using leaf protein extracts from wild type and be single mutants (Atbe2 and Atbe3 mutant lines) and by different combinations of recombinant proteins. Chain length distribution (CLD) patterns of the formed glucans were irrespective of SSI and BE isoforms origin and still independent of assay conditions. Furthermore, we show that all SS isoforms (SSI-SSIV) were able to interact with BEs and form branched glucans. However, only SSI/BEs generated a polymodal distribution of glucans which was similar to CLD pattern detected in amylopectin of Arabidopsis leaf starch. We discuss the impact of the SSI/BEs interplay for the CLD pattern of amylopectin.

Indexed as

1,4-alpha-Glucan Branching EnzymeAmylopectinArabidopsisArabidopsis ProteinsGene Expression Regulation, PlantIsoenzymesPlant LeavesRecombinant ProteinsSignal TransductionStarchStarch Synthase1,4-alpha-Glucan Branching EnzymeAmylopectinArabidopsis ProteinsIsoenzymesRecombinant ProteinsStarchStarch Synthase

Identifiers

PMID25014622
PMCPMC4094495
OpenAlexW2039558800

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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.