Membrane-bound class III peroxidases: Identification, biochemical properties and sequence analysis of isoenzymes purified from maize (Zea mays L.) roots

2008 ◽  
Vol 71 (4) ◽  
pp. 412-424 ◽  
Author(s):  
Angela Mika ◽  
Friedrich Buck ◽  
Sabine Lüthje
Keyword(s):  
Zea Mays ◽  
Sequence Analysis ◽  
Zea Mays L ◽  
Biochemical Properties ◽  
Class Iii ◽  
Membrane Bound ◽  
Class Iii Peroxidases

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

Inhibition of Maize (Zea mays L.) Root Plasma Membrane-Bound Redox Activities by Coumarins

1994 ◽  
Vol 49 (7-8) ◽  
pp. 447-452 ◽  
Author(s):  
Sabine Lüthje ◽  
José A. Gonzaléz-Reyes ◽  
Placido Navas ◽  
Olaf Döring ◽  
Michael Böttger
Keyword(s):  
Zea Mays ◽  
Plasma Membrane ◽  
Zea Mays L ◽  
Membrane Vesicles ◽  
Dependent Manner ◽  
Plasma Membrane Vesicles ◽  
Two Phase ◽  
Concentration Dependent Manner ◽  
Oxidoreductase Activity ◽  
Membrane Bound

Modulation of plasma membrane-bound NADH:hexacyanoferrate III oxidoreductase activities by dicumarol and warfarin was investigated with plasma membrane vesicles of Zea mays L. (cv. Sil Anjou 18) roots, prepared by aqueous two phase partitioning. Vesicles were about 65% right-side out orientated as demonstrated by enzyme latency of vanadate sensitive ATPase activity. Dicumarol or warfarin, respectively, inhibited NADH:hexacyanoferrate III oxidoreductase activity in a concentration-dependent manner and inhibition could be reversed partially by addition of quinones

scholarly journals Membrane-bound guaiacol peroxidases from maize (Zea mays L.) roots are regulated by methyl jasmonate, salicylic acid, and pathogen elicitors

2009 ◽  
Vol 61 (3) ◽  
pp. 831-841 ◽  
Author(s):  
Angela Mika ◽  
Marike Johanne Boenisch ◽  
David Hopff ◽  
Sabine Lüthje
Keyword(s):  
Zea Mays ◽  
Salicylic Acid ◽  
Methyl Jasmonate ◽  
Zea Mays L ◽  
Membrane Bound

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 Responses of soil physical, chemical and biochemical properties to short-term impact of tillage in an alfisol under maize (Zea mays L.) cultivation

2019 ◽  
Author(s):  
Ajoke Christianah Adegaye ◽  
Solomon Adejoro ◽  
Segun Oladele ◽  
Daniel Arotupin ◽  
Stephen Ojeniyi
Keyword(s):  
Zea Mays ◽  
Zea Mays L ◽  
Chemical Properties ◽  
Biochemical Properties ◽  
Short Term ◽  
Physical Chemical ◽  
The Impact ◽  
Treatment Application ◽  
Herbicide Glyphosate ◽  
Term Field

A short-term field and laboratory experiment was conducted to assess the impact of four traditional tillage methods on the physical, chemical and biochemical properties of a sandy clay loam alfisol under maize (Zea mays L.) cultivation following a fallow period of five years. Treatments included slash only (SO), slash +burn (SB), slash+ ridge (SR) and herbicide (glyphosate) application (HA) at the recommended rate of 2 L/ha-1. Results from the statistical analysis of data from this study showed inconsistent trends of tillage treatments on soil physical properties. However, slash +burn (SB) tillage significantly (p < 0.05) enhanced chemical properties such as the soil pH, available P, exchangeable K+, Ca2+, and Mg2+ compared to their respective values before treatment application in the two years under study. Amongst the treatments, slash + burn (SB) tillage further exerted the most significant (P ≤ 0.05) effect on urease, L-asparaginase, L-glutaminase, dehydrogenase, acid and alkaline phosphatase activities, but recorded the least values for amidase and β-glucosidase activities in soil. Results from this study therefore, suggest that SB tillage treatment was beneficial to the soil environment as it has proven to be more promising and effective for enhancing the selected soil quality indicators on the soil type due to quick mineralization and release of bound nutrients present in the soil and litter.

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