The Barley Grain Thioredoxin System - an Update

Overview

Journal Front Plant Sci

Date 2013 Jun 5

PMID 23734159

Citations 3

Authors

Per Hagglund

Olof Bjornberg

Nicolas Navrot

Johanne Morch Jensen

Kenji Maeda

Kristine Kirkensgaard

Azar Shahpiri

Abida Sultan

Jakob Bunkenborg

Frank Gubler

Jose Maria Barrero

Anette Henriksen

Christine Finnie

Birte Svensson

Affiliations

Soon will be listed here.

Abstract

Thioredoxin (Trx) reduces disulfide bonds and play numerous important functions in plants. In cereal seeds, cytosolic h-type Trx facilitates the release of energy reserves during the germination process and is recycled by NADPH-dependent Trx reductase. This review presents a summary of the research conducted during the last 10 years to elucidate the structure and function of the barley seed Trx system at the molecular level combined with proteomic approaches to identify target proteins.

Citing Articles

Redox-dependent interaction between thaumatin-like protein and β-glucan influences malting quality of barley.

Singh S, Tripathi R, Lemaux P, Buchanan B, Singh J Proc Natl Acad Sci U S A. 2017; 114(29):7725-7730.

PMID: 28634304 PMC: 5530668. DOI: 10.1073/pnas.1701824114.

Replacement of threonine-55 with glycine decreases the reduction rate of OsTrx20 by glutathione.

Roodgar-Nashta M, Shahpiri A Mol Biol Res Commun. 2017; 6(1):33-40.

PMID: 28447047 PMC: 5396813.

Functional and structural characterization of plastidic starch phosphorylase during barley endosperm development.

Cuesta-Seijo J, Ruzanski C, Krucewicz K, Meier S, Hagglund P, Svensson B PLoS One. 2017; 12(4):e0175488.

PMID: 28407006 PMC: 5391026. DOI: 10.1371/journal.pone.0175488.

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