The amelioration of aluminium toxicity by silicon in higher plants: Solution chemistry or an in planta mechanism?

1998 ◽  
Vol 104 (4) ◽  
pp. 608-614 ◽  
Author(s):  
Kay M. Cocker ◽  
David E. Evans ◽  
Martin J. Hodson
Keyword(s):  
Higher Plants ◽  
Aluminium Toxicity ◽  
Solution Chemistry ◽  
In Planta

scholarly journals Genome-wide alternative splicing profiling in the fungal plant pathogen Sclerotinia sclerotiorum during the colonization of diverse host families

2020 ◽  
Author(s):  
Heba M. M. Ibrahim ◽  
Stefan Kusch ◽  
Marie Didelon ◽  
Sylvain Raffaele
Keyword(s):  
Alternative Splicing ◽  
Sclerotinia Sclerotiorum ◽  
Plant Pathogen ◽  
Host Plants ◽  
Higher Plants ◽  
Pathogenic Fungus ◽  
Differentially Expressed ◽  
Cell Protein ◽  
In Planta ◽  
Alternative Transcripts

AbstractSclerotinia sclerotiorum is a notorious generalist plant pathogen that threatens more than 600 host plants including wild and cultivated species. The molecular bases underlying the broad compatibility of S. sclerotiorum with its hosts is not fully elucidated. In contrast to higher plants and animals, alternative splicing (AS) is not well studied in plant pathogenic fungi. AS is a common regulated cellular process that increases cell protein and RNA diversity. In this study, we annotated spliceosome genes in the genome of S. sclerotiorum and characterized their expression in vitro and during the colonization of six host species. Several spliceosome genes were differentially expressed in planta, suggesting that AS was altered during infection. Using stringent parameters, we identified 1,487 S. sclerotiorum genes differentially expressed in planta and exhibiting alternative transcripts. The most common AS events during the colonization of all plants were retained introns and alternative 3′ receiver site. We identified S. sclerotiorum genes expressed in planta for which (i) the relative accumulation of alternative transcripts varies according to the host being colonized and (ii) alternative transcripts harbor distinct protein domains. This notably included 42 genes encoding predicted secreted proteins showing high confidence AS events. This study indicates that AS events are taking place in the plant pathogenic fungus S. sclerotiorum during the colonization of host plants and could generate functional diversity in the repertoire of proteins secreted by S. sclerotiorum during infection.

Element distribution in red spruce (Picearubens) fine roots; evidence for aluminium toxicity at Whiteface Mountain

1992 ◽  
Vol 22 (8) ◽  
pp. 1132-1138 ◽  
Author(s):  
Hedda Schlegel ◽  
Robert G. Amundson ◽  
Aloys Hüttermann
Keyword(s):  
New York ◽  
Fine Roots ◽  
Aluminium Toxicity ◽  
High Elevation ◽  
Element Distribution ◽  
Solution Chemistry ◽  
Red Spruce ◽  
Ion Distribution ◽  
Root Cortex ◽  
Whiteface Mountain

To determine the element distribution in fine roots of red spruce (Picearubens Sarg.) at a high-elevation decline site on Whiteface Mountain, New York, fine-root samples were collected and analysed by X-ray microanalysis. Aluminium was found in very high concentrations in the root cortex, but could not be detected in stelar tissues. In contrast, magnesium was found only in the central cylinder in low amounts. The calcium concentration in the cortex was low, but was higher in the stele. Aluminium has been shown to interfere with cation uptake by blocking exchange sites in the cortical apoplast. Thus these results strongly suggest that the low foliar magnesium and calcium contents of the declining red spruce trees are driven by aluminium-induced inhibition of magnesium and calcium uptake. Soil solution chemistry, ion distribution in fine roots, and foliar ion contents at Whiteface Mountain were compared with equivalent data from other forest sites as well as with data from controlled studies on spruce seedlings. These data suggest that aluminium toxicity contributes to red spruce decline at Whiteface Mountain.

scholarly journals Modeling of asymmetric division of somatic cell in protoplasts culture of higher plants

2020 ◽  
Vol 11 (2) ◽  
pp. 255-265
Author(s):  
S. I. Kondratenko ◽  
T. P. Pasternak ◽  
O. P. Samovol ◽  
O. M. Mogilna ◽  
O. V. Sergienko
Keyword(s):  
Cell Division ◽  
Osmotic Stress ◽  
Growth Regulators ◽  
Nutrient Medium ◽  
Higher Plants ◽  
Asymmetric Division ◽  
Cycle Phase ◽  
In Planta ◽  
Selection Of

The key result of the work is the selection of factors for the cultivation of protoplasts of higher plants in vitro, which allowed induction of asymmetrical cell division during the first cell cycle phase. Gibberellin has been proved to be one of the main cofactors of asymmetric division of plant cells. The objects of research were plants of the following cultivars aseptically grown in hormone-free MS medium: tobacco (Nicotiana tabacum L.), SR-1 line; Arabidopsis thaliana var. columbia (L.) Heynh; potato (Solanum tuberosum L.), Zarevo cultivar; cultivated white head cabbage (Brassica oleraceae var. capitata L.) of the following varieties: Kharkivska zymnia, Ukrainska osin, Yaroslavna, Lika, Lesya, Bilosnizhka, Dithmarscher Früher, Iyunskarannya; rape (Brassica napus L.) of Shpat cultivar; winter radish (Raphanus sativus L.) of Odessa-5 cultivar. In experiments with mesophilic and hypocotyl protoplasts of the above-mentioned plant species it has been proved that short-term osmotic stress within 16–18 hours being combined with subsequent introduction of high doses of gibberellin GK3 (1 mg/L) into the modified liquid nutrient media TM and SW led to the occurrence of pronounced morphological traits of cytodifferentiation already at the initial stages of the development of mitotically active cells in a number of higher plants. Meanwhile, in all analyzed species, there was observed the division of the initial genetically homogeneous population of mitotically active cells into two types of asymmetric division: by the type of division of the mother cell into smaller daughter cells and by the type of the first asymmetric division of the zygotic embryo in planta. In this case, the first type of asymmetric division occurred during unusual cytomorphism of the mother cells: a pronounced heart-shaped form even before the first division, which is inherent in the morphology of somatic plant embryo in vitro at the heart-shaped stage. A particular study of the effect of osmotic stress influencing protoplasts of various cultivars of white cabbage, isolated from hypocotyls of 7–9 day etiolated seedlings, revealed quite a typical consistent pattern: the acquisition and maintenance of the axis of symmetry in growing microcolonies occurred without extra exogenous gibberellin (GK3), which was added to the nutrient medium earlier. While analyzing the effect of growth regulators on the formation of microcolonies with traits of structural organization, the conclusion was made regarding the commonality of the revealed morphogenetic reactions of cells within the culture of protoplasts of higher plants in vitro with similar reactions studied earlier on other plants, both in vitro and in planta. Modeling of asymmetric cell division in protoplast culture in vitro has become possible by carrying out a balanced selection of growth regulators as well as their coordinated application through time along with changes in osmotic pressure of a nutrient medium.

scholarly journals The GluTR-binding protein is the heme-binding factor for feedback control of glutamyl-tRNA reductase

eLife ◽  
2019 ◽  
Vol 8 ◽  
Author(s):  
Andreas S Richter ◽  
Claudia Banse ◽  
Bernhard Grimm
Keyword(s):  
Translational Control ◽  
Aminolevulinic Acid ◽  
Higher Plants ◽  
Binding Protein ◽  
In Planta ◽  
Clp Protease ◽  
Functional Link ◽  
Photosynthetic Eukaryotes ◽  
Dependent Inhibition ◽  
Long Time

Synthesis of 5-aminolevulinic acid (ALA) is the rate-limiting step in tetrapyrrole biosynthesis in land plants. In photosynthetic eukaryotes and many bacteria, glutamyl-tRNA reductase (GluTR) is the most tightly controlled enzyme upstream of ALA. Higher plants possess two GluTR isoforms: GluTR1 is predominantly expressed in green tissue, and GluTR2 is constitutively expressed in all organs. Although proposed long time ago, the molecular mechanism of heme-dependent inhibition of GluTR in planta has remained elusive. Here, we report that accumulation of heme, induced by feeding with ALA, stimulates Clp-protease-dependent degradation of Arabidopsis GluTR1. We demonstrate that binding of heme to the GluTR-binding protein (GBP) inhibits interaction of GBP with the N-terminal regulatory domain of GluTR1, thus making it accessible to the Clp protease. The results presented uncover a functional link between heme content and the post-translational control of GluTR stability, which helps to ensure adequate availability of chlorophyll and heme.

scholarly journals BcXyl, a β-xylosidase Isolated from Brunfelsia Calycina Flowers with Anthocyanin-β-glycosidase Activity

2019 ◽  
Vol 20 (6) ◽  
pp. 1423
Author(s):  
Boyu Dong ◽  
Honghui Luo ◽  
Bin Liu ◽  
Wenjun Li ◽  
Shaojian Ou ◽  
...  
Keyword(s):  
High Performance ◽  
Higher Plants ◽  
Peptide Sequencing ◽  
Glycoside Hydrolase Family ◽  
In Planta ◽  
Chromatography Analysis ◽  
Glycosidic Bonds ◽  
Hydrolysis Of ◽  
Hydrolase Family ◽  
Anthocyanin Degradation

Brunfelsia calycina flowers lose anthocyanins rapidly and are therefore well suited for the study of anthocyanin degradation mechanisms, which are unclear in planta. Here, we isolated an anthocyanin-β-glycosidase from B. calycina petals. The MS/MS (Mass Spectrometry) peptide sequencing showed that the enzyme (72 kDa) was a β-xylosidase (BcXyl). The enzyme showed high activity to p-Nitrophenyl-β-d-galactopyranoside (pNPGa) and p-Nitrophenyl-β-d-xylopyranoside (pNPX), while no activity to p-Nitrophenyl-β-d-glucopyranoside (pNPG) or p-Nitrophenyl-β-D-mannopyranoside (pNPM) was seen. The optimum temperature of BcXyl was 40 °C and the optimum pH was 5.0. The enzyme was strongly inhibited by 1 mM D-gluconate and Ag+. HPLC (High Performance Liquid Chromatography) analysis showed that BcXyl catalyzed the degradation of an anthocyanin component of B. calycina, and the release of xylose and galactose due to hydrolysis of glycosidic bonds by BcXyl was detected by GC (Gas Chromatography) /MS. A full-length mRNA sequence (2358 bp) of BcXyl (NCBI No. MK411219) was obtained and the deduced protein sequence shared conserved domains with two anthocyanin-β-glycosidases (Bgln and BadGluc, characterized in fungi). BcXyl, Bgln and BadGluc belong to AB subfamily of Glycoside hydrolase family 3. Similar to BcPrx01, an anthocyanin-degradation-related Peroxidase (POD), BcXyl was dramatically activated at the stage at which the rapid anthocyanin degradation occurred. Taken together, we suggest that BcXyl may be the first anthocyanin-β-glycosidase identified in higher plants.

scholarly journals Arabidopsis PII Proteins Form Characteristic Foci in Chloroplasts Indicating Novel Properties in Protein Interaction and Degradation

2021 ◽  
Author(s):  
Natalie Krieger ◽  
Kai-Florian Pastryk ◽  
Karl Forchhammer ◽  
Üner Kolukisaoglu
Keyword(s):  
Higher Plants ◽  
Regulatory Protein ◽  
Physiological Role ◽  
In Planta ◽  
Pii Protein ◽  
Starting Point ◽  
Pii Proteins ◽  
First Time ◽  
Novel Protein

The PII protein is an evolutionary highly conserved regulatory protein from bacteria to higher plants. In bacteria it modulates the activity of several enzymes, transporters and regulatory factors by interacting with them and thereby regulating important metabolic hubs like carbon/nitrogen homeostasis. More than two decades ago the PII protein was characterized for the first time in plants, but its physiological role is still not sufficiently resolved. To gain more insights into the function of this protein, we investigated the interaction behaviour of AtPII with candidate proteins by BiFC and FRET/FLIM in planta and with GFP/RFP traps in vitro. In the course of these studies we found that AtPII interacts in chloroplasts with itself as well as with known interactors like NAGK in dot-like aggregates, which we named PII foci. In these novel protein aggregates AtPII interacts also with yet unknown partners, which are known to be involved in plastidic protein degradation. Further studies revealed that the C-terminal part of AtPII is crucial for the formation of PII foci. Altogether, the presented results indicate a novel mode of interaction for PII proteins with other proteins in plants, which may be a new starting point for the elucidation of physiological functions of PII proteins in plants.

scholarly journals N-terminal β-strand underpins biochemical specialization of an ATG8 isoform

2018 ◽  
Author(s):  
Erin K. Zess ◽  
Cassandra Jensen ◽  
Neftaly Cruz-Mireles ◽  
Juan Carlos De la Concepcion ◽  
Jan Sklenar ◽  
...  
Keyword(s):  
Protein Interaction ◽  
Higher Plants ◽  
Plant Evolution ◽  
Single Amino Acid ◽  
Plant Proteins ◽  
In Planta ◽  
Amino Acid Polymorphism ◽  
Biochemical Basis

AbstractATG8 is a highly-conserved ubiquitin-like protein that modulates autophagy pathways by binding autophagic membranes and numerous proteins, including cargo receptors and core autophagy components. Throughout plant evolution, ATG8 has expanded from a single protein in algae to multiple isoforms in higher plants. However, the degree to which ATG8 isoforms have functionally specialized to bind distinct proteins remains unclear. Here, we describe a comprehensive protein-protein interaction resource, obtained using in planta immunoprecipitation followed by mass spectrometry, to define the potato ATG8 interactome. We discovered that ATG8 isoforms bind distinct sets of plant proteins with varying degrees of overlap. This prompted us to define the biochemical basis of ATG8 specialization by comparing two potato ATG8 isoforms using both in vivo protein interaction assays and in vitro quantitative binding affinity analyses. These experiments revealed that the N-terminal β-strand—and, in particular, a single amino acid polymorphism—underpins binding specificity to the substrate PexRD54 by shaping the hydrophobic pocket that accommodates this protein’s ATG8 interacting motif. Additional proteomics experiments indicated that the N-terminal β-strand shapes the ATG8 interactor profiles, defining interaction specificity with about 80 plant proteins. Our findings are consistent with the view that ATG8 isoforms comprise a layer of specificity in the regulation of selective autophagy pathways in plants.

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