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Thiol-based redox homeostasis and signalling

Authors: --- --- --- --- et al.
Book Series: Frontiers Research Topics ISSN: 16648714 ISBN: 9782889192847 Year: Pages: 235 DOI: 10.3389/978-2-88919-284-7 Language: English
Publisher: Frontiers Media SA
Subject: Botany --- Physiology --- Science (General)
Added to DOAB on : 2015-12-10 11:59:07
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Abstract

In contrast to the situation in heterotrophic organisms, plant genomes code for a significantly larger number of oxidoreductases such as thioredoxins (TRXs) and glutaredoxins (GRXs). These proteins provide a biochemical mechanism that allows the rapid and reversible activation or deactivation of protein functions in response to changing environmental conditions, as oxidative conditions caused by excessive photosynthesis. Indeed, owing to the fact that cysteines are sensitive to oxidation, TRXs and GRXs play an essential role in controlling the redox state of protein thiol groups. These redox-dependent post-translational modifications have proven to be critical for many cellular functions constituting regulatory, signalling or protective mechanisms. The articles contained in this Research Topic provide timely overviews and new insights into thiol-dependent redox regulation mechanisms with a focus on TRX- and GRX-based reduction systems in plants. The different contexts discussed take into account physiological, developmental and environmental conditions.

Thioredoxin and Glutaredoxin Systems

Authors: ---
ISBN: 9783038978367 / 9783038978374 Year: Pages: 280 DOI: 10.3390/books978-3-03897-837-4 Language: eng
Publisher: MDPI - Multidisciplinary Digital Publishing Institute
Subject: Science (General) --- Biology
Added to DOAB on : 2019-06-26 08:44:06
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This Special Issue features recent data concerning thioredoxins and glutaredoxins from various biological systems, including bacteria, mammals, and plants. Four of the sixteen articles are review papers that deal with the regulation of development of the effect of hydrogen peroxide and the interactions between oxidants and reductants, the description of methionine sulfoxide reductases, detoxification enzymes that require thioredoxin or glutaredoxin, and the response of plants to cold stress, respectively. This is followed by eleven research articles that focus on a reductant of thioredoxin in bacteria, a thioredoxin reductase, and a variety of plant and bacterial thioredoxins, including the m, f, o, and h isoforms and their targets. Various parameters are studied, including genetic, structural, and physiological properties of these systems. The redox regulation of monodehydroascorbate reductase, aminolevulinic acid dehydratase, and cytosolic isocitrate dehydrogenase could have very important consequences in plant metabolism. Also, the properties of the mitochondrial o-type thioredoxins and their unexpected capacity to bind iron–sulfur center (ISC) structures open new developments concerning the redox mitochondrial function and possibly ISC assembly in mitochondria. The final paper discusses interesting biotechnological applications of thioredoxin for breadmaking.

Keywords

methionine --- methionine sulfoxide --- methionine sulfoxide reductase --- physiological function --- protein --- plant --- repair --- redox homeostasis --- signaling --- stress --- mitochondria --- thioredoxin --- iron–sulfur cluster --- redox regulation --- ALAD --- tetrapyrrole biosynthesis --- redox control --- thioredoxins --- posttranslational modification --- chlorophyll --- redox regulation --- thioredoxin --- ferredoxin-thioredoxin reductase --- chloroplast --- H2O2 --- redox signalling --- development --- regeneration --- adult stem cells --- metazoan --- cyanobacteria --- thioredoxin --- photosynthesis --- redox active site --- thioredoxin --- disulfide --- flavin --- NADPH --- X-ray crystallography --- SAXS --- methanoarchaea --- chilling stress --- cold temperature --- posttranslational modification --- regulation --- ROS --- thiol redox network --- thioredoxin --- thioredoxin --- Calvin-Benson cycle --- photosynthesis --- carbon fixation --- chloroplast --- macromolecular crystallography --- protein-protein recognition --- electrostatic surface --- Chlamydomonas reinhardtii --- thioredoxin --- glutaredoxin --- legume plant --- symbiosis --- redox homeostasis --- stress --- thioredoxin --- monodehydroascorbate reductase --- water stress --- protein oxidation --- antioxidants --- ascorbate --- glutathione --- wheat --- thioredoxin --- thioredoxin reductase --- baking --- redox --- dough rheology --- protein oxidation --- methionine oxidation --- methionine sulfoxide reductases --- oxidized protein repair --- ageing --- Chlamydomonas reinhardtii --- cysteine alkylation --- cysteine reactivity --- MALDI-TOF mass spectrometry --- thioredoxin --- X-ray crystallography --- Isocitrate dehydrogenase --- glutathionylation --- nitrosylation --- glutaredoxin --- Arabidopsis thaliana --- thioredoxins --- plastidial --- specificity --- function --- proteomic --- photosynthesis --- Calvin cycle --- n/a

Physiological Responses to Abiotic and Biotic Stress in Forest Trees

Authors: ---
ISBN: 9783039215140 / 9783039215157 Year: Pages: 294 DOI: 10.3390/books978-3-03921-515-7 Language: eng
Publisher: MDPI - Multidisciplinary Digital Publishing Institute
Subject: Technology (General) --- General and Civil Engineering --- Environmental Engineering
Added to DOAB on : 2019-12-09 11:49:15
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Abstract

As sessile organisms, plants have to cope with a multitude of natural and anthropogenic forms of stress in their environment. Due to their longevity, this is of particular significance for trees. As a consequence, trees develop an orchestra of resilience and resistance mechanisms to biotic and abiotic stresses in order to support their growth and development in a constantly changing atmospheric and pedospheric environment. The objective of this Special Issue of Forests is to summarize state-of-art knowledge and report the current progress on the processes that determine the resilience and resistance of trees from different zonobiomes as well as all forms of biotic and abiotic stress from the molecular to the whole tree level.

Keywords

drought --- mid-term --- non-structural carbohydrate --- soluble sugar --- starch --- Pinus massoniana --- salinity --- Carpinus betulus --- morphological indices --- gas exchange --- osmotic adjustment substances --- antioxidant enzyme activity --- ion relationships --- Populus simonii Carr. (poplar) --- intrinsic water-use efficiency --- tree rings --- basal area increment --- long-term drought --- hydrophilic polymers --- Stockosorb --- Luquasorb --- Konjac glucomannan --- photosynthesis --- ion relation --- Fagus sylvatica L. --- Abies alba Mill. --- N nutrition --- mixed stands --- pure stands --- soil N --- water relations --- 24-epiBL application --- salt stress --- ion contents --- chloroplast ultrastructure --- photosynthesis --- Robinia pseudoacacia L. --- elevation gradient --- forest type --- growth --- leaf properties --- Pinus koraiensis Sieb. et Zucc. --- Heterobasidion parviporum --- Heterobasidion annosum --- Norway spruce --- disturbance --- water availability --- pathogen --- infection --- Carpinus turczaninowii --- salinity treatments --- ecophysiology --- photosynthetic responses --- organic osmolytes --- ion homeostasis --- antioxidant enzymes --- glutaredoxin --- subcellular localization --- expression --- tapping panel dryness --- defense response --- rubber tree --- Ca2+ signal --- drought stress --- living cell --- Moso Bamboo (Phyllostachys edulis) --- plasma membrane Ca2+ channels --- signal network --- Aleppo pine --- Greece --- photosynthesis --- water potential --- ?13C --- sap flow --- canopy conductance --- climate --- molecular cloning --- functional analysis --- TCP --- DELLA --- GA-signaling pathway --- Fraxinus mandshurica Rupr. --- wood formation --- abiotic stress --- nutrition --- gene regulation --- tree --- bamboo forest --- cold stress --- physiological response --- silicon fertilization --- plant tolerance --- reactive oxygen species --- antioxidant activity --- proline --- Populus euphratica --- salt stress --- salicylic acid --- malondialdehyde --- differentially expressed genes --- n/a

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