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Chloroplast thioredoxin systems: prospects for improving photosynthesis.

Authors :
Nikkanen L
Toivola J
Diaz MG
Rintamäki E
Source :
Philosophical transactions of the Royal Society of London. Series B, Biological sciences [Philos Trans R Soc Lond B Biol Sci] 2017 Sep 26; Vol. 372 (1730).
Publication Year :
2017

Abstract

Thioredoxins (TRXs) are protein oxidoreductases that control the structure and function of cellular proteins by cleavage of a disulphide bond between the side chains of two cysteine residues. Oxidized thioredoxins are reactivated by thioredoxin reductases (TR) and a TR-dependent reduction of TRXs is called a thioredoxin system. Thiol-based redox regulation is an especially important mechanism to control chloroplast proteins involved in biogenesis, in regulation of light harvesting and distribution of light energy between photosystems, in photosynthetic carbon fixation and other biosynthetic pathways, and in stress responses of plants. Of the two plant plastid thioredoxin systems, the ferredoxin-dependent system relays reducing equivalents from photosystem I via ferredoxin and ferredoxin-thioredoxin reductase (FTR) to chloroplast proteins, while NADPH-dependent thioredoxin reductase (NTRC) forms a complete thioredoxin system including both reductase and thioredoxin domains in a single polypeptide. Chloroplast thioredoxins transmit environmental light signals to biochemical reactions, which allows fine tuning of photosynthetic processes in response to changing environmental conditions. In this paper we focus on the recent reports on specificity and networking of chloroplast thioredoxin systems and evaluate the prospect of improving photosynthetic performance by modifying the activity of thiol regulators in plants.This article is part of the themed issue 'Enhancing photosynthesis in crop plants: targets for improvement'.<br /> (© 2017 The Authors.)

Details

Language :
English
ISSN :
1471-2970
Volume :
372
Issue :
1730
Database :
MEDLINE
Journal :
Philosophical transactions of the Royal Society of London. Series B, Biological sciences
Publication Type :
Academic Journal
Accession number :
28808108
Full Text :
https://doi.org/10.1098/rstb.2016.0474