Evidence map›Paper›PMID 31494665›Full record

ArticleJournal of experimental botany2020

Expression of starch-binding factor CBM20 in barley plastids controls the number of starch granules and the level of CO2 fixation.

Yingxin Zhong, Domenico Sagnelli, Henrik Bak Topbjerg, Harald Hasler-Sheetal, Olga Agata Andrzejczak, Kourosh Hooshmand, René Gislum, Dong Jiang, Ian Max Møller, Andreas Blennow and 1 more

Open access · hybridAbstract read
In one paragraph

Article in Journal of experimental botany, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 41% 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

2 citing papers in PubMed, 4 citations in OpenAlex.

  1. Novel Design of an α-Amylase with an N-Terminal CBM20 inMolecules (Basel, Switzerland) · 2023
    Article
  2. Review
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

11 authors at 4 institutions in 2 countries.

Yingxin ZhongDepartment of Molecular Biology and Genetics, Aarhus University, Flakkebjerg, Forsøgsvej 1, 4200 Slagelse, Denmark.
Domenico SagnelliDepartment of Molecular Biology and Genetics, Aarhus University, Flakkebjerg, Forsøgsvej 1, 4200 Slagelse, Denmark.
Henrik Bak TopbjergDepartment of Agroecology, Aarhus University, Flakkebjerg, Forsøgsvej 1, 4200 Slagelse, Denmark.
Harald Hasler-SheetalDepartment of Molecular Biology and Genetics, Aarhus University, Flakkebjerg, Forsøgsvej 1, 4200 Slagelse, Denmark.
Olga Agata AndrzejczakDepartment of Molecular Biology and Genetics, Aarhus University, Flakkebjerg, Forsøgsvej 1, 4200 Slagelse, Denmark.
Kourosh HooshmandDepartment of Molecular Biology and Genetics, Aarhus University, Flakkebjerg, Forsøgsvej 1, 4200 Slagelse, Denmark.
René GislumDepartment of Agroecology, Aarhus University, Flakkebjerg, Forsøgsvej 1, 4200 Slagelse, Denmark.
Dong JiangNational Technique Innovation Center for Regional Wheat Production/Key Laboratory of Crop Physiology and Ecology in Southern China, Ministry of Agriculture/National Engineering and technology Center for Information Agriculture, Nanjing Agricultural University, Nanjing, P. R. China.
Ian Max MøllerDepartment of Molecular Biology and Genetics, Aarhus University, Flakkebjerg, Forsøgsvej 1, 4200 Slagelse, Denmark.
Andreas BlennowDepartment of Plant and Environmental Sciences, Copenhagen University, Frederiksberg, Denmark.
Kim Henrik HebelstrupDepartment of Molecular Biology and Genetics, Aarhus University, Flakkebjerg, Forsøgsvej 1, 4200 Slagelse, Denmark.
Aarhus University · DKUniversity of Copenhagen · DKNanjing Agricultural University · CNUniversity of Southern Denmark · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The biosynthesis of starch granules in plant plastids is coordinated by the orchestrated action of transferases, hydrolases, and dikinases. These enzymes either contain starch-binding domain(s) themselves, or are dependent on direct interactions with co-factors containing starch-binding domains. As a means to competitively interfere with existing starch-protein interactions, we expressed the protein module Carbohydrate-Binding Motif 20 (CBM20), which has a very high affinity for starch, ectopically in barley plastids. This interference resulted in an increase in the number of starch granules in chloroplasts and in formation of compound starch granules in grain amyloplasts, which is unusual for barley. More importantly, we observed a photosystem-independent inhibition of CO2 fixation, with a subsequent reduced growth rate and lower accumulation of carbohydrates with effects throughout the metabolome, including lower accumulation of transient leaf starch. Our results demonstrate the importance of endogenous starch-protein interactions for controlling starch granule morphology and number, and plant growth, as substantiated by a metabolic link between starch-protein interactions and control of CO2 fixation in chloroplasts.

Indexed as

Carbon CycleCarbon DioxideHordeumPlant ProteinsPlastidsStarchCarbon DioxidePlant ProteinsStarchBarley, Hordeum vulgare, photosynthesisstarch metabolismstarch-protein interactions

Identifiers

PMID31494665
PMCPMC6913705
OpenAlexW2973116416

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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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.