scholarly journals Hypoxia-Responsive Class III Peroxidases in Maize Roots: Soluble and Membrane-Bound Isoenzymes

2020 ◽  
Vol 21 (22) ◽  
pp. 8872
Author(s):  
Anne Hofmann ◽  
Stefanie Wienkoop ◽  
Sönke Harder ◽  
Fabian Bartlog ◽  
Sabine Lüthje
Keyword(s):  
Cross Sections ◽  
Phenylpropanoid Pathway ◽  
Guaiacol Peroxidase ◽  
Class Iii ◽  
Low Oxygen ◽  
Aerenchyma Formation ◽  
2D Page ◽  
Membrane Bound ◽  
Class Iii Peroxidases ◽  
Scavenging Enzymes

Flooding induces low-oxygen environments (hypoxia or anoxia) that lead to energy disruption and an imbalance of reactive oxygen species (ROS) production and scavenging enzymes in plants. The influence of hypoxia on roots of hydroponically grown maize (Zea mays L.) plants was investigated. Gene expression (RNA Seq and RT-qPCR) and proteome (LC–MS/MS and 2D-PAGE) analyses were used to determine the alterations in soluble and membrane-bound class III peroxidases under hypoxia. Gel-free peroxidase analyses of plasma membrane-bound proteins showed an increased abundance of ZmPrx03, ZmPrx24, ZmPrx81, and ZmPr85 in stressed samples. Furthermore, RT-qPCR analyses of the corresponding peroxidase genes revealed an increased expression. These peroxidases could be separated with 2D-PAGE and identified by mass spectrometry. An increased abundance of ZmPrx03 and ZmPrx85 was determined. Further peroxidases were identified in detergent-insoluble membranes. Co-regulation with a respiratory burst oxidase homolog (Rboh) and key enzymes of the phenylpropanoid pathway indicates a function of the peroxidases in membrane protection, aerenchyma formation, and cell wall remodeling under hypoxia. This hypothesis was supported by the following: (i) an elevated level of hydrogen peroxide and aerenchyma formation; (ii) an increased guaiacol peroxidase activity in membrane fractions of stressed samples, whereas a decrease was observed in soluble fractions; and (iii) alterations in lignified cells, cellulose, and suberin in root cross-sections.

scholarly journals Membrane-Bound Class III Peroxidases: Unexpected Enzymes with Exciting Functions

2018 ◽  
Vol 19 (10) ◽  
pp. 2876 ◽  
Author(s):  
Sabine Lüthje ◽  
Teresa Martinez-Cortes
Keyword(s):  
Plasma Membranes ◽  
Secretory Pathway ◽  
In Silico Analysis ◽  
Class Iii ◽  
Membrane Repair ◽  
Protein Protein Interaction ◽  
Thale Cress ◽  
Membrane Bound ◽  
Class Iii Peroxidases ◽  
Detergent Resistant Membrane

Class III peroxidases are heme-containing proteins of the secretory pathway with a high redundance and versatile functions. Many soluble peroxidases have been characterized in great detail, whereas only a few studies exist on membrane-bound isoenzymes. Membrane localization of class III peroxidases has been demonstrated for tonoplast, plasma membrane and detergent resistant membrane fractions of different plant species. In silico analysis revealed transmembrane domains for about half of the class III peroxidases that are encoded by the maize (Zea mays) genome. Similar results have been found for other species like thale-cress (Arabidopsis thaliana), barrel medic (Medicago truncatula) and rice (Oryza sativa). Besides this, soluble peroxidases interact with tonoplast and plasma membranes by protein–protein interaction. The topology, spatiotemporal organization, molecular and biological functions of membrane-bound class III peroxidases are discussed. Besides a function in membrane protection and/or membrane repair, additional functions have been supported by experimental data and phylogenetics.

Phylogeny, topology, structure and functions of membrane-bound class III peroxidases in vascular plants

2011 ◽  
Vol 72 (10) ◽  
pp. 1124-1135 ◽  
Author(s):  
Sabine Lüthje ◽  
Claudia-Nicole Meisrimler ◽  
David Hopff ◽  
Benjamin Möller
Keyword(s):  
Vascular Plants ◽  
Class Iii ◽  
Topology Structure ◽  
Membrane Bound ◽  
Class Iii Peroxidases ◽  
Structure And Functions

scholarly journals Activity of Class III Peroxidases in the Defense of Cotton to Bacterial Blight

2003 ◽  
Vol 16 (11) ◽  
pp. 1030-1038 ◽  
Author(s):  
E. Delannoy ◽  
A. Jalloul ◽  
K. Assigbetsé ◽  
P. Marmey ◽  
J. P. Geiger ◽  
...  
Keyword(s):  
Oxidative Burst ◽  
Bacterial Blight ◽  
Xanthomonas Campestris ◽  
Time Course ◽  
Hypersensitive Reaction ◽  
Guaiacol Peroxidase ◽  
Class Iii ◽  
Transcript Accumulation ◽  
Class Iii Peroxidases

Cotton cotyledons displayed a hypersensitive reaction (HR) in the cultivar Réba B50 after infiltration with the aviru-lent race 18 from Xanthomonas campestris pv. malvacearum. Two sets of peroxidases were associated with the HR time course. Early but transient accumulation of peroxidase in material encapsulating the bacteria in intercellular areas was observed by immunocytochemistry at 3 h postinfection and coincided with the oxidative burst. Total guaiacol-peroxidase activity was highly increased in cells undergoing HR, from 12 h after treatment. Molecular characterization of seven cloned peroxidase genes revealed highly conserved B, D, and F domains, with similarities to plant class III peroxidases. Analysis of gene expression showed variation in transcript accumulation during both compatible (race 20) and incompatible interactions for four of these genes: pod2, pod3, pod4, and pod6.Pod4 and pod6 were more intensely up-regulated during resistance than during disease and in the control, while pod3 was specifically down-regulated during the HR after the oxidative burst. Pod2 was induced by pathogen infection and weakly stimulated in the control. These data suggest that cotton peroxidases may have various functions in the defense response to Xanthomonas infections.

Spindle shaped bodies in foveolar cones of the baboon retina

1989 ◽  
Vol 47 ◽  
pp. 960-961
Author(s):  
W. Krebs ◽  
I. Krebs
Keyword(s):  
Cross Sections ◽  
Inclusion Bodies ◽  
Photoreceptor Cells ◽  
Papio Anubis ◽  
Retinal Photoreceptor ◽  
Age Related ◽  
Cone Cells ◽  
Membrane Bound ◽  
Oriented Parallel ◽  
Shaped Inclusion

Various inclusion bodies occur in vertebrate retinal photoreceptor cells. Most of them are membrane bound and associated with phagocytosis or they are age related residual bodies. We found an additional inclusion body in foveal cone cells of the baboon (Papio anubis) retina.The eyes of a 15 year old baboon were fixed by immersion in cacodylate buffered glutaraldehyde (2%)/formaldehyde (2%) as described in detail elsewhere . Pieces of retina from various locations, including the fovea, were embedded in epoxy resin such that radial or tangential sections could be cut.Spindle shaped inclusion bodies were found in the cytoplasm of only foveal cones. They were abundant in the inner segments, close to the external limiting membrane (Fig. 1). But they also occurred in the outer fibers, the perikarya, and the inner fibers (Henle’s fibers) of the cone cells. The bodies were between 0.5 and 2 μm long. Their central diameter was 0.2 to 0. 3 μm. They always were oriented parallel to the long axis of the cone cells. In longitudinal sections (Figs. 2,3) they seemed to have a fibrous skeleton that, in cross sections, turned out to consist of plate-like (Fig.4) and tubular profiles (Fig. 5).

scholarly journals Genome-wide identification and analysis of class III peroxidases in Betula pendula

BMC Genomics ◽  
2021 ◽  
Vol 22 (1) ◽  
Author(s):  
Kewei Cai ◽  
Huixin Liu ◽  
Song Chen ◽  
Yi Liu ◽  
Xiyang Zhao ◽  
...  
Keyword(s):  
Stress Responses ◽  
Betula Pendula ◽  
Expression Patterns ◽  
Class Iii ◽  
Physiological Processes ◽  
Plant Life ◽  
Genome Wide ◽  
Plant Life Cycle ◽  
Class Iii Peroxidases ◽  
And Function

Abstract Background Class III peroxidases (POD) proteins are widely present in the plant kingdom that are involved in a broad range of physiological processes including stress responses and lignin polymerization throughout the plant life cycle. At present, POD genes have been studied in Arabidopsis, rice, poplar, maize and Chinese pear, but there are no reports on the identification and function of POD gene family in Betula pendula. Results We identified 90 nonredundant POD genes in Betula pendula. (designated BpPODs). According to phylogenetic relationships, these POD genes were classified into 12 groups. The BpPODs are distributed in different numbers on the 14 chromosomes, and some BpPODs were located sequentially in tandem on chromosomes. In addition, we analyzed the conserved domains of BpPOD proteins and found that they contain highly conserved motifs. We also investigated their expression patterns in different tissues, the results showed that some BpPODs might play an important role in xylem, leaf, root and flower. Furthermore, under low temperature conditions, some BpPODs showed different expression patterns at different times. Conclusions The research on the structure and function of the POD genes in Betula pendula plays a very important role in understanding the growth and development process and the molecular mechanism of stress resistance. These results lay the theoretical foundation for the genetic improvement of Betula pendula.

scholarly journals Enzyme-catalyzed Mechanism of Isoniazid Activation in Class I and Class III Peroxidases

2004 ◽  
Vol 279 (37) ◽  
pp. 39000-39009 ◽  
Author(s):  
Roberta Pierattelli ◽  
Lucia Banci ◽  
Nigel A. J. Eady ◽  
Jacques Bodiguel ◽  
Jamie N. Jones ◽  
...  
Keyword(s):  
Class I ◽  
Class Iii ◽  
Class Iii Peroxidases

Pyrophosphate as an alternative energy currency in plants

2021 ◽  
Vol 478 (8) ◽  
pp. 1515-1524
Author(s):  
Abir U. Igamberdiev ◽  
Leszek A. Kleczkowski
Keyword(s):  
Metabolic Pathways ◽  
Energy Efficient ◽  
Alternative Energy ◽  
Plant Cells ◽  
Atp Synthesis ◽  
Continuous Operation ◽  
Low Oxygen ◽  
Pyruvate Phosphate Dikinase ◽  
Oxygen Stress ◽  
Membrane Bound

In the conditions of [Mg2+] elevation that occur, in particular, under low oxygen stress and are the consequence of the decrease in [ATP] and increase in [ADP] and [AMP], pyrophosphate (PPi) can function as an alternative energy currency in plant cells. In addition to its production by various metabolic pathways, PPi can be synthesized in the combined reactions of pyruvate, phosphate dikinase (PPDK) and pyruvate kinase (PK) by so-called PK/PPDK substrate cycle, and in the reverse reaction of membrane-bound H+-pyrophosphatase, which uses the energy of electrochemical gradients generated on tonoplast and plasma membrane. The PPi can then be consumed in its active forms of MgPPi and Mg2PPi by PPi-utilizing enzymes, which require an elevated [Mg2+]. This ensures a continuous operation of glycolysis in the conditions of suppressed ATP synthesis, keeping metabolism energy efficient and less dependent on ATP.

Class III Peroxidases

2013 ◽  
pp. 687-706 ◽  
Author(s):  
Sabine Lüthje ◽  
Claudia-Nicole Meisrimler ◽  
David Hopff ◽  
Tim Schütze ◽  
Jenny Köppe ◽  
...  
Keyword(s):  
Class Iii ◽  
Class Iii Peroxidases
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