scholarly journals Post-Translational Modifications of Nuclear Proteins in the Response of Plant Cells to Abiotic Stresses

10.5772/23822 ◽  
2011 ◽  
Author(s):  
Jennifer Dahan ◽  
Emmanuel Koen ◽  
Agnes Dutartre ◽  
Olivier Lamotte ◽  
Stephane Bourque
Keyword(s):  
Abiotic Stresses ◽  
Plant Cells ◽  
Nuclear Proteins ◽  
Post Translational Modifications

scholarly journals Actin–binding proteins in the Arabidopsis genome database: properties of functionally distinct plant actin–depolymerizing factors/cofilins

2002 ◽  
Vol 357 (1422) ◽  
pp. 791-798 ◽  
Author(s):  
Patrick J. Hussey ◽  
Ellen G. Allwood ◽  
Andrei P. Smertenko
Keyword(s):  
Abiotic Stresses ◽  
Cytoplasmic Streaming ◽  
Binding Proteins ◽  
Plant Cells ◽  
Actin Binding ◽  
Biotic And Abiotic Stresses ◽  
Actin Binding Proteins ◽  
Genome Database ◽  
Cellular Processes ◽  
Stimulus Responsive

The plant actin cytoskeleton is a highly dynamic, fibrous structure essential in many cellular processes including cell division and cytoplasmic streaming. This structure is stimulus responsive, being affected by internal stimuli, by biotic and abiotic stresses mediated in signal transduction pathways by actin–binding proteins. The completion of the Arabidopsis genome sequence has allowed a comparative identification of many actin–binding proteins. However, not all are conserved in plants, which possibly reflects the differences in the processes involved in morphogenesis between plant and other cells. Here we have searched for the Arabidopsis equivalents of 67 animal/fungal actin–binding proteins and show that 36 are not conserved in plants. One protein that is conserved across phylogeny is actin–depolymerizing factor or cofilin and we describe our work on the activity of vegetative tissue and pollen–specific isoforms of this protein in plant cells, concluding that they are functionally distinct.

scholarly journals Hydrogen Sulfide: A Robust Combatant against Abiotic Stresses in Plants

Hydrogen ◽  
2021 ◽  
Vol 2 (3) ◽  
pp. 319-342
Author(s):  
Kanika Khanna ◽  
Nandni Sharma ◽  
Sandeep Kour ◽  
Mohd. Ali ◽  
Puja Ohri ◽  
...  
Keyword(s):  
Hydrogen Sulfide ◽  
Abiotic Stresses ◽  
Cysteine Residues ◽  
Plant Signaling ◽  
Plant Tolerance ◽  
Gaseous State ◽  
Post Translational Modifications ◽  
Adverse Conditions ◽  
Physiological Processes ◽  
Near Future

Hydrogen sulfide (H2S) is predominantly considered as a gaseous transmitter or signaling molecule in plants. It has been known as a crucial player during various plant cellular and physiological processes and has been gaining unprecedented attention from researchers since decades. They regulate growth and plethora of plant developmental processes such as germination, senescence, defense, and maturation in plants. Owing to its gaseous state, they are effectively diffused towards different parts of the cell to counterbalance the antioxidant pools as well as providing sulfur to cells. H2S participates actively during abiotic stresses and enhances plant tolerance towards adverse conditions by regulation of the antioxidative defense system, oxidative stress signaling, metal transport, Na+/K+ homeostasis, etc. They also maintain H2S-Cys-cycle during abiotic stressed conditions followed by post-translational modifications of cysteine residues. Besides their role during abiotic stresses, crosstalk of H2S with other biomolecules such as NO and phytohormones (abscisic acid, salicylic acid, melatonin, ethylene, etc.) have also been explored in plant signaling. These processes also mediate protein post-translational modifications of cysteine residues. We have mainly highlighted all these biological functions along with proposing novel relevant issues that are required to be addressed further in the near future. Moreover, we have also proposed the possible mechanisms of H2S actions in mediating redox-dependent mechanisms in plant physiology.

Nitric oxide and hydrogen sulfide modulate the NADPH-generating enzymatic system in higher plants

2020 ◽  
Author(s):  
Francisco J Corpas ◽  
Salvador González-Gordo ◽  
José M Palma
Keyword(s):  
Nitric Oxide ◽  
Hydrogen Sulfide ◽  
Plant Cells ◽  
Redox Status ◽  
Signal Molecules ◽  
Tyrosine Nitration ◽  
Enzymatic System ◽  
Post Translational Modifications ◽  
Cellular Redox ◽  
Wide Range

Abstract Nitric oxide (NO) and hydrogen sulfide (H2S) are two key molecules in plant cells that participate, directly or indirectly, as regulators of protein functions through derived post-translational modifications, mainly tyrosine nitration, S-nitrosation, and persulfidation. These post-translational modifications allow the participation of both NO and H2S signal molecules in a wide range of cellular processes either physiological or under stressful circumstances. NADPH participates in cellular redox status and it is a key cofactor necessary for cell growth and development. It is involved in significant biochemical routes such as fatty acid, carotenoid and proline biosynthesis, and the shikimate pathway, as well as in cellular detoxification processes including the ascorbate–glutathione cycle, the NADPH-dependent thioredoxin reductase (NTR), or the superoxide-generating NADPH oxidase. Plant cells have diverse mechanisms to generate NADPH by a group of NADP-dependent oxidoreductases including ferredoxin-NADP reductase (FNR), NADP-glyceraldehyde-3-phosphate dehydrogenase (NADP-GAPDH), NADP-dependent malic enzyme (NADP-ME), NADP-dependent isocitrate dehydrogenase (NADP-ICDH), and both enzymes of the oxidative pentose phosphate pathway, designated as glucose-6-phosphate dehydrogenase (G6PDH) and 6-phosphogluconate dehydrogenase (6PGDH). These enzymes consist of different isozymes located in diverse subcellular compartments (chloroplasts, cytosol, mitochondria, and peroxisomes) which contribute to the NAPDH cellular pool. We provide a comprehensive overview of how post-translational modifications promoted by NO (tyrosine nitration and S-nitrosation), H2S (persulfidation), and glutathione (glutathionylation), affect the cellular redox status through regulation of the NADP-dependent dehydrogenases.

scholarly journals Phytohormones Regulate Accumulation of Osmolytes Under Abiotic Stress

Biomolecules ◽  
2019 ◽  
Vol 9 (7) ◽  
pp. 285 ◽  
Author(s):  
Anket Sharma ◽  
Babar Shahzad ◽  
Vinod Kumar ◽  
Sukhmeen Kaur Kohli ◽  
Gagan Preet Singh Sidhu ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Abiotic Stresses ◽  
Compatible Solutes ◽  
Plant Cells ◽  
Normal Growth ◽  
Cellular Damage ◽  
Oxygen Species ◽  
Osmolyte Accumulation ◽  
Cellular Machinery ◽  
Underlying Mechanisms

Plants face a variety of abiotic stresses, which generate reactive oxygen species (ROS), and ultimately obstruct normal growth and development of plants. To prevent cellular damage caused by oxidative stress, plants accumulate certain compatible solutes known as osmolytes to safeguard the cellular machinery. The most common osmolytes that play crucial role in osmoregulation are proline, glycine-betaine, polyamines, and sugars. These compounds stabilize the osmotic differences between surroundings of cell and the cytosol. Besides, they also protect the plant cells from oxidative stress by inhibiting the production of harmful ROS like hydroxyl ions, superoxide ions, hydrogen peroxide, and other free radicals. The accumulation of osmolytes is further modulated by phytohormones like abscisic acid, brassinosteroids, cytokinins, ethylene, jasmonates, and salicylic acid. It is thus important to understand the mechanisms regulating the phytohormone-mediated accumulation of osmolytes in plants during abiotic stresses. In this review, we have discussed the underlying mechanisms of phytohormone-regulated osmolyte accumulation along with their various functions in plants under stress conditions.

scholarly journals Manipulation of Ascorbate Biosynthetic, Recycling, and Regulatory Pathways for Improved Abiotic Stress Tolerance in Plants

2020 ◽  
Vol 21 (5) ◽  
pp. 1790 ◽  
Author(s):  
Ronan C. Broad ◽  
Julien P. Bonneau ◽  
Roger P. Hellens ◽  
Alexander A.T. Johnson
Keyword(s):  
Abiotic Stress ◽  
Stress Tolerance ◽  
Abiotic Stresses ◽  
Abiotic Stress Tolerance ◽  
Plant Cells ◽  
Water Soluble ◽  
Upstream Open Reading Frame ◽  
Limiting Factors ◽  
Crop Species ◽  
Regulatory Pathways

Abiotic stresses, such as drought, salinity, and extreme temperatures, are major limiting factors in global crop productivity and are predicted to be exacerbated by climate change. The overproduction of reactive oxygen species (ROS) is a common consequence of many abiotic stresses. Ascorbate, also known as vitamin C, is the most abundant water-soluble antioxidant in plant cells and can combat oxidative stress directly as a ROS scavenger, or through the ascorbate–glutathione cycle—a major antioxidant system in plant cells. Engineering crops with enhanced ascorbate concentrations therefore has the potential to promote broad abiotic stress tolerance. Three distinct strategies have been utilized to increase ascorbate concentrations in plants: (i) increased biosynthesis, (ii) enhanced recycling, or (iii) modulating regulatory factors. Here, we review the genetic pathways underlying ascorbate biosynthesis, recycling, and regulation in plants, including a summary of all metabolic engineering strategies utilized to date to increase ascorbate concentrations in model and crop species. We then highlight transgene-free strategies utilizing genome editing tools to increase ascorbate concentrations in crops, such as editing the highly conserved upstream open reading frame that controls translation of the GDP-L-galactose phosphorylase gene.

Chromatin architecture and functions: the role(s) of poly(ADP-RIBOSE) polymerase and poly(ADPribosyl)ation of nuclear proteins

2005 ◽  
Vol 83 (3) ◽  
pp. 396-404 ◽  
Author(s):  
Maria Rosaria Faraone-Mennella
Keyword(s):  
Apoptotic Cell ◽  
Histone Variants ◽  
Controlling Factors ◽  
Nuclear Proteins ◽  
Dna Breaks ◽  
Specific Expression ◽  
Cellular Division ◽  
Protein Targets ◽  
Post Translational Modifications ◽  
Parp 1

Epigenetic states that allow chromatin fidelity inheritance can be mediated by several factors. One of them, histone variants and their modifications (including acetylation, methylation, phosphorylation, poly(ADP-ribosyl)ation, and ubiquitylation) create distinct patterns of signals read by other proteins, and are strictly related to chromatin remodelling, which is necessary for the specific expression of a gene, and for DNA repair, recombination, and replication. In the framework of chromatin-controlling factors, the poly(ADP-ribosyl)ation of nuclear proteins, catalysed by poly(ADP-ribose)polymerases (PARPs), has been implicated in the regulation of both physiological and pathological events (gene expression/amplification, cellular division/differentiation, DNA replication, malignant transformation, and apoptotic cell death). The involvement of PARPs in this scenario has raised doubts about the epigenetic value of poly(ADP-ribosyl)ation, because it is generally activated after DNA damage. However, one emerging view suggests that both the product of this reaction, poly(ADP-ribose), and PARPs, particularly PARP 1, play a fundamental role in recruiting protein targets to specific sites and (or) in interacting physically with structural and regulatory factors, through highly reproducible and inheritable mechanisms, often independent of DNA breaks. The interplay of PARPs with protein factors, and the combinatorial effect of poly(ADPribosyl)ation with other post-translational modifications has shed new light on the potential and versatility of this dynamic reaction.Key words: chromatin, epigenetic, poly(ADP-ribose), PARP.

Protamine-DNA interaction

1978 ◽  
Vol 36 (2) ◽  
pp. 200-201
Author(s):  
D.P. Bazett-Jones ◽  
F.P. Ottensmeyer
Keyword(s):  
Small Volume ◽  
Double Helix ◽  
Dna Interaction ◽  
Dark Field ◽  
Sperm Head ◽  
Nuclear Proteins ◽  
Field Electron Microscopy ◽  
Dark Field Electron ◽  
Dna Double Helix ◽  
Positively Charged

Dark field electron microscopy has been used for the study of the structure of individual macromolecules with a resolution to at least the 5Å level. The use of this technique has been extended to the investigation of structure of interacting molecules, particularly the interaction between DNA and fish protamine, a class of basic nuclear proteins of molecular weight 4,000 daltons.Protamine, which is synthesized during spermatogenesis, binds to chromatin, displaces the somatic histones and wraps up the DNA to fit into the small volume of the sperm head. It has been proposed that protamine, existing as an extended polypeptide, winds around the minor groove of the DNA double helix, with protamine's positively-charged arginines lining up with the negatively-charged phosphates of DNA. However, viewing protamine as an extended protein is inconsistent with the results obtained in our laboratory.

Sign in / Sign up

Export Citation Format

Share Document