scholarly journals Plant Protein O-Arabinosylation

2021 ◽  
Vol 12 ◽  
Author(s):  
Bent Larsen Petersen ◽  
Cora A. MacAlister ◽  
Peter Ulvskov
Keyword(s):  
Cell Wall ◽  
Stress Responses ◽  
Secretory Pathway ◽  
Peptide Hormones ◽  
Common Denominator ◽  
Small Peptide ◽  
Structural Cell ◽  
Additional Layer ◽  
Wide Range ◽  
Diverse Groups

A wide range of proteins with diverse functions in development, defense, and stress responses areO-arabinosylated at hydroxyprolines (Hyps) within distinct amino acid motifs of continuous stretches of Hyps, as found in the structural cell wall extensins, or at non-continuous Hyps as, for example, found in small peptide hormones and a variety of plasma membrane proteins involved in signaling. PlantO-glycosylation relies on hydroxylation of Prolines to Hyps in the protein backbone, mediated by prolyl-4-hydroxylase (P4H) which is followed byO-glycosylation of the Hyp C4-OH group by either galactosyltransferases (GalTs) or arabinofuranosyltranferases (ArafTs) yielding either Hyp-galactosylation or Hyp-arabinosylation. A subset of the P4H enzymes with putative preference to hydroxylation of continuous prolines and presumably all ArafT enzymes needed for synthesis of the substituted arabinose chains of one to four arabinose units, have been identified and functionally characterized. Truncated root-hair phenotype is one common denominator of mutants of Hyp formation and Hyp-arabinosylation glycogenes, which act on diverse groups ofO-glycosylated proteins, e.g., the small peptide hormones and cell wall extensins. Dissection of different substrate derived effects may not be regularly feasible and thus complicate translation from genotype to phenotype. Recently, lack of proper arabinosylation on arabinosylated proteins has been shown to influence their transport/fate in the secretory pathway, hinting to an additional layer of functionality ofO-arabinosylation. Here, we provide an update on the prevalence and types ofO-arabinosylated proteins and the enzymatic machinery responsible for their modifications.

scholarly journals N-Acetylglucosamine Regulates Morphogenesis and Virulence Pathways in Fungi

2019 ◽  
Vol 6 (1) ◽  
pp. 8 ◽  
Author(s):  
Kyunghun Min ◽  
Shamoon Naseem ◽  
James B. Konopka
Keyword(s):  
Cell Wall ◽  
Stress Responses ◽  
Hyphal Growth ◽  
Amino Sugar ◽  
Model Organisms ◽  
Animal Cells ◽  
Epigenetic Switch ◽  
Wide Range ◽  
Extracellular Environment

N-acetylglucosamine (GlcNAc) is being increasingly recognized for its ability to stimulate cell signaling. This amino sugar is best known as a component of cell wall peptidoglycan in bacteria, cell wall chitin in fungi and parasites, exoskeletons of arthropods, and the extracellular matrix of animal cells. In addition to these structural roles, GlcNAc is now known to stimulate morphological and stress responses in a wide range of organisms. In fungi, the model organisms Saccharomyces cerevisiae and Schizosaccharomyces pombe lack the ability to respond to GlcNAc or catabolize it, so studies with the human pathogen Candida albicans have been providing new insights into the ability of GlcNAc to stimulate cellular responses. GlcNAc potently induces C. albicans to transition from budding to filamentous hyphal growth. It also promotes an epigenetic switch from White to Opaque cells, which differ in morphology, metabolism, and virulence properties. These studies have led to new discoveries, such as the identification of the first eukaryotic GlcNAc transporter. Other results have shown that GlcNAc can induce signaling in C. albicans in two ways. One is to act as a signaling molecule independent of its catabolism, and the other is that its catabolism can cause the alkalinization of the extracellular environment, which provides an additional stimulus to form hyphae. GlcNAc also induces the expression of virulence genes in the C. albicans, indicating it can influence pathogenesis. Therefore, this review will describe the recent advances in understanding the role of GlcNAc signaling pathways in regulating C. albicans morphogenesis and virulence.

scholarly journals The Fast and the Furious: Golgi Contact Sites

Contact ◽  
2021 ◽  
Vol 4 ◽  
pp. 251525642110344
Author(s):  
Yotam David ◽  
Inês G. Castro ◽  
Maya Schuldiner
Keyword(s):  
Stress Responses ◽  
Metabolic Pathways ◽  
Secretory Pathway ◽  
Current Knowledge ◽  
Close Apposition ◽  
Cellular Functions ◽  
Future Directions ◽  
Contact Sites ◽  
The Past ◽  
Wide Range

Contact sites are areas of close apposition between two membranes that coordinate nonvesicular communication between organelles. Such interactions serve a wide range of cellular functions from regulating metabolic pathways to executing stress responses and coordinating organelle inheritance. The past decade has seen a dramatic increase in information on certain contact sites, mostly those involving the endoplasmic reticulum. However, despite its central role in the secretory pathway, the Golgi apparatus and its contact sites remain largely unexplored. In this review, we discuss the current knowledge of Golgi contact sites and share our thoughts as to why Golgi contact sites are understudied. We also highlight what exciting future directions may exist in this emerging field.

scholarly journals Sed1p Is a Major Cell Wall Protein ofSaccharomyces cerevisiae in the Stationary Phase and Is Involved in Lytic Enzyme Resistance

1998 ◽  
Vol 180 (13) ◽  
pp. 3381-3387 ◽  
Author(s):  
Hitoshi Shimoi ◽  
Hiroshi Kitagaki ◽  
Hisanobu Ohmori ◽  
Yuzuru Iimura ◽  
Kiyoshi Ito
Keyword(s):  
Cell Wall ◽  
Stationary Phase ◽  
Cell Walls ◽  
Secretory Pathway ◽  
Signal Sequence ◽  
Sodium Dodecyl ◽  
Cell Wall Protein ◽  
Lytic Enzyme ◽  
Cell Wall Proteins ◽  
Structural Cell

ABSTRACT A 260-kDa structural cell wall protein was purified from sodium dodecyl sulfate-treated cell walls of Saccharomyces cerevisiae by incubation with Rarobacter faecitabidusprotease I, which is a yeast-lytic enzyme. Amino acid sequence analysis revealed that this protein is the product of the SED1 gene.SED1 was formerly identified as a multicopy suppressor oferd2, which encodes a protein involved in retrieval of luminal endoplasmic reticulum proteins from the secretory pathway. Sed1p is very rich in threonine and serine and, like other structural cell wall proteins, contains a putative signal sequence for the addition of a glycosylphosphatidylinositol anchor. However, the fact that Sed1p, unlike other cell wall proteins, has six cysteines and seven putative N-glycosylation sites suggests that Sed1p belongs to a new family of cell wall proteins. Epitope-tagged Sed1p was detected in a β-1,3-glucanase extract of cell walls by immunoblot analysis, suggesting that Sed1p is a glucanase-extractable cell wall protein. The expression of Sed1p mRNA increased in the stationary phase and was accompanied by an increase in the Sed1p content of cell walls. Disruption of SED1 had no effect on exponentially growing cells but made stationary-phase cells sensitive to Zymolyase. These results indicate that Sed1p is a major structural cell wall protein in stationary-phase cells and is required for lytic enzyme resistance.

New insights on Laminaria digitata ultrastructure through combined conventional chemical fixation and cryofixation

2021 ◽  
Vol 0 (0) ◽  
Author(s):  
Christos Katsaros ◽  
Sophie Le Panse ◽  
Gillian Milne ◽  
Carl J. Carrano ◽  
Frithjof Christian Küpper
Keyword(s):  
Cell Wall ◽  
General Structure ◽  
Raw Material ◽  
Rocky Shores ◽  
Chemical Fixation ◽  
Laminaria Digitata ◽  
Vegetative Cells ◽  
Biological Studies ◽  
New Findings ◽  
Wide Range

Abstract The objective of the present study is to examine the fine structure of vegetative cells of Laminaria digitata using both chemical fixation and cryofixation. Laminaria digitata was chosen due to its importance as a model organism in a wide range of biological studies, as a keystone species on rocky shores of the North Atlantic, its use of iodide as a unique inorganic antioxidant, and its significance as a raw material for the production of alginate. Details of the fine structural features of vegetative cells are described, with particular emphasis on the differences between the two methods used, i.e. conventional chemical fixation and freeze-fixation. The general structure of the cells was similar to that already described, with minor differences between the different cell types. An intense activity of the Golgi system was found associated with the thick external cell wall, with large dictyosomes from which numerous vesicles and cisternae are released. An interesting type of cisternae was found in the cryofixed material, which was not visible with the chemical fixation. These are elongated structures, in sections appearing tubule-like, close to the external cell wall or to young internal walls. An increased number of these structures was observed near the plasmodesmata of the pit fields. They are similar to the “flat cisternae” found associated with the forming cytokinetic diaphragm of brown algae. Their possible role is discussed. The new findings of this work underline the importance of such combined studies which reveal new data not known until now using the old conventional methods. The main conclusion of the present study is that cryofixation is the method of choice for studying Laminaria cytology by transmission electron microscopy.

scholarly journals amontillado, the Drosophila Homolog of the Prohormone Processing Protease PC2, Is Required During Embryogenesis and Early Larval Development

Genetics ◽  
2003 ◽  
Vol 163 (1) ◽  
pp. 227-237 ◽  
Author(s):  
Lowell Y M Rayburn ◽  
Holly C Gooding ◽  
Semil P Choksi ◽  
Dhea Maloney ◽  
Ambrose R Kidd ◽  
...  
Keyword(s):  
Larval Development ◽  
Secretory Pathway ◽  
Larval Growth ◽  
Peptide Hormones ◽  
Complementation Group ◽  
Prohormone Processing ◽  
Complementation Groups ◽  
Regulated Secretory Pathway ◽  
Processing Protease ◽  
Larval Molt

Abstract Biosynthesis of most peptide hormones and neuropeptides requires proteolytic excision of the active peptide from inactive proprotein precursors, an activity carried out by subtilisin-like proprotein convertases (SPCs) in constitutive or regulated secretory pathways. The Drosophila amontillado (amon) gene encodes a homolog of the mammalian PC2 protein, an SPC that functions in the regulated secretory pathway in neuroendocrine tissues. We have identified amon mutants by isolating ethylmethanesulfonate (EMS)-induced lethal and visible mutations that define two complementation groups in the amon interval at 97D1 of the third chromosome. DNA sequencing identified the amon complementation group and the DNA sequence change for each of the nine amon alleles isolated. amon mutants display partial embryonic lethality, are defective in larval growth, and arrest during the first to second instar larval molt. Mutant larvae can be rescued by heat-shock-induced expression of the amon protein. Rescued larvae arrest at the subsequent larval molt, suggesting that amon is also required for the second to third instar larval molt. Our data indicate that the amon proprotein convertase is required during embryogenesis and larval development in Drosophila and support the hypothesis that AMON acts to proteolytically process peptide hormones that regulate hatching, larval growth, and larval ecdysis.

scholarly journals The Craterostigma plantagineum protein kinase CpWAK1 interacts with pectin and integrates different environmental signals in the cell wall

Planta ◽  
2021 ◽  
Vol 253 (5) ◽  
Author(s):  
Peilei Chen ◽  
Valentino Giarola ◽  
Dorothea Bartels
Keyword(s):  
Cell Wall ◽  
Stress Responses ◽  
Expression Profiles ◽  
Phylogenetic Analyses ◽  
Cell Wall Protein ◽  
Biological Processes ◽  
Environmental Signals ◽  
High Affinity ◽  
Craterostigma Plantagineum ◽  
Receptor Kinases

Abstract Main conclusion The cell wall protein CpWAK1 interacts with pectin, participates in decoding cell wall signals, and induces different downstream responses. Abstract Cell wall-associated protein kinases (WAKs) are transmembrane receptor kinases. In the desiccation-tolerant resurrection plant Craterostigma plantagineum, CpWAK1 has been shown to be involved in stress responses and cell expansion by forming a complex with the C. plantagineum glycine-rich protein1 (CpGRP1). This prompted us to extend the studies of WAK genes in C. plantagineum. The phylogenetic analyses of WAKs from C. plantagineum and from other species suggest that these genes have been duplicated after species divergence. Expression profiles indicate that CpWAKs are involved in various biological processes, including dehydration-induced responses and SA- and JA-related reactions to pathogens and wounding. CpWAK1 shows a high affinity for “egg-box” pectin structures. ELISA assays revealed that the binding of CpWAKs to pectins is modulated by CpGRP1 and it depends on the apoplastic pH. The formation of CpWAK multimers is the prerequisite for the CpWAK–pectin binding. Different pectin extracts lead to opposite trends of CpWAK–pectin binding in the presence of Ca2+ at pH 8. These observations demonstrate that CpWAKs can potentially discriminate and integrate cell wall signals generated by diverse stimuli, in concert with other elements, such as CpGRP1, pHapo, Ca2+[apo], and via the formation of CpWAK multimers.

scholarly journals Structural, Evolutionary, and Functional Analysis of the Protein O-Mannosyltransferase Family in Pathogenic Fungi

2021 ◽  
Vol 7 (5) ◽  
pp. 328
Author(s):  
María Dolores Pejenaute-Ochoa ◽  
Carlos Santana-Molina ◽  
Damien P. Devos ◽  
José Ignacio Ibeas ◽  
Alfonso Fernández-Álvarez
Keyword(s):  
Functional Analysis ◽  
Secretory Pathway ◽  
Pathogenic Fungi ◽  
Fungal Pathogenesis ◽  
Post Translational Modification ◽  
Key Factors ◽  
Wide Range ◽  
Single Deletion ◽  
Asymmetrical Impact ◽  
Substrate Proteins

Protein O-mannosyltransferases (Pmts) comprise a group of proteins that add mannoses to substrate proteins at the endoplasmic reticulum. This post-translational modification is important for the faithful transfer of nascent glycoproteins throughout the secretory pathway. Most fungi genomes encode three O-mannosyltransferases, usually named Pmt1, Pmt2, and Pmt4. In pathogenic fungi, Pmts, especially Pmt4, are key factors for virulence. Although the importance of Pmts for fungal pathogenesis is well established in a wide range of pathogens, questions remain regarding certain features of Pmts. For example, why does the single deletion of each pmt gene have an asymmetrical impact on host colonization? Here, we analyse the origin of Pmts in fungi and review the most important phenotypes associated with Pmt mutants in pathogenic fungi. Hence, we highlight the enormous relevance of these glycotransferases for fungal pathogenic development.

scholarly journals Antimicrobial Nodule-Specific Cysteine-Rich Peptides Induce Membrane Depolarization-Associated Changes in the Transcriptome of Sinorhizobium meliloti

2013 ◽  
Vol 79 (21) ◽  
pp. 6737-6746 ◽  
Author(s):  
Hilda Tiricz ◽  
Attila Szűcs ◽  
Attila Farkas ◽  
Bernadett Pap ◽  
Rui M. Lima ◽  
...  
Keyword(s):  
Stress Responses ◽  
Sinorhizobium Meliloti ◽  
Antimicrobial Agents ◽  
Cellular Functions ◽  
Gram Positive ◽  
Content Type ◽  
Gram Positive Bacteria ◽  
Peptide Family ◽  
Wide Range ◽  
Natural Target

ABSTRACTLeguminous plants establish symbiosis with nitrogen-fixing alpha- and betaproteobacteria, collectively called rhizobia, which provide combined nitrogen to support plant growth. Members of the inverted repeat-lacking clade of legumes impose terminal differentiation on their endosymbiotic bacterium partners with the help of the nodule-specific cysteine-rich (NCR) peptide family composed of close to 600 members. Among the few tested NCR peptides, cationic ones had antirhizobial activity measured by reduction or elimination of the CFU and uptake of the membrane-impermeable dye propidium iodide. Here, the antimicrobial spectrum of two of these peptides, NCR247 and NCR335, was investigated, and their effect on the transcriptome of the natural targetSinorhizobium melilotiwas characterized. Both peptides were able to kill quickly a wide range of Gram-negative and Gram-positive bacteria; however, their spectra were only partially overlapping, and differences were found also in their efficacy on given strains, indicating that the actions of NCR247 and NCR335 might be similar though not identical. Treatment ofS. meliloticultures with either peptide resulted in a quick downregulation of genes involved in basic cellular functions, such as transcription-translation and energy production, as well as upregulation of genes involved in stress and oxidative stress responses and membrane transport. Similar changes provoked mainly in Gram-positive bacteria by antimicrobial agents were coupled with the destruction of membrane potential, indicating that it might also be a common step in the bactericidal actions of NCR247 and NCR335.

Peroxidase: a multifunctional enzyme in grapevines

2003 ◽  
Vol 30 (6) ◽  
pp. 577 ◽  
Author(s):  
Alfonso Ros Barceló ◽  
Federico Pomar ◽  
Matías López-Serrano ◽  
Maria Angeles Pedreño
Keyword(s):  
Cell Wall ◽  
Metabolic Regulation ◽  
Trichoderma Viride ◽  
Visible Spectrum ◽  
H2o2 Production ◽  
Class Iii ◽  
Absorption Bands ◽  
Peroxidase Isoenzyme ◽  
Wide Range ◽  
Uv C

Peroxidases are heme-containing enzymes that catalyse the one-electron oxidation of several substrates at the expense of H2O2. They are probably encoded by a large multigene family in grapevines, and therefore show a high degree of polymorphism. Grapevine peroxidases are glycoproteins of high thermal stability, whose molecular weight usually ranges from 35 to 45 kDa. Their visible spectrum shows absorption bands characteristic of high-spin class III peroxidases. Grapevine peroxidases are capable of accepting a wide range of natural compounds as substrates, such as the cell wall protein extensin, plant growth regulators such as IAA, and phenolics such as benzoic acids, stilbenes, flavonols, cinnamyl alcohols and anthocyanins. They are located in cell walls and vacuoles. These locations are in accordance with their key role in determining the final cell wall architecture, especially regarding lignin deposition and extensin insolubilization, and the turnover of vacuolar phenolic metabolites, a task that also forms part of the molecular program of disease resistance. Although peroxidase is a constitutive enzyme in grapevines, its levels are strongly modulated during plant cell development and in response to both biotic and abiotic environmental factors. To gain an insight into the metabolic regulation of peroxidase, several authors have studied how grapevine peroxidase and H2O2 levels change in response to a changing environment. Nevertheless, the results obtained are not always easy to interpret. Despite such difficulties, the response of the peroxidase–H2O2 system to both UV-C radiation and Trichoderma viride elicitors is worthy of study. Both UV-C and T. viride elicitors induce specific changes in peroxidase isoenzyme / H2O2 levels, which result in specific changes in grapevine physiology and metabolism. In the case of T. viride-elicited grapevine cells, they show a particular mechanism for H2O2 production, in which NADPH oxidase-like activities are apparently not involved. However, they offer a unique system whereby the metabolic regulation of peroxidase by H2O2, with all its cross-talks and downstream signals, may be elegantly dissected.

Spectrophotometry of Aqueous HNO3, H2SO4, and DCIO4 from 25° to 250°C

1968 ◽  
Vol 22 (5) ◽  
pp. 545-548 ◽  
Author(s):  
W. C. Waggener ◽  
A. J. Weinberger ◽  
R. W. Stoughton
Keyword(s):  
Cell Wall ◽  
Corrosion Products ◽  
Spectral Measurements ◽  
Wide Range ◽  
General Program ◽  
Cell Window ◽  
Temperature And Pressure

Dilute nitric, sulfuric, and perchloric acids are applicable as solvents for spectrophotometry up to 250°C over the following ranges: 0 to 1.0 f HNO3 from 0.6 to 1.2 μ; 0 to 0.2 f H2SO4 from 0.25 to 1.2 μ; and 0 to 1.0 f DClO4 from 0.25 to 1.8 μ. Each of these acids reacts measurably with the titanium cell wall and the sapphire windows at rates which increase with acidity and temperature. This corrosion affects the spectral measurements as a function of time and is associated with deterioration of cell window surfaces and the presence in the sample of dissolved and suspended corrosion products. These results are part of our more general program for the development of equipment and technique for routine spectrophotometry of pure liquids and solutions over a wide range of temperature and pressure.

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