Plasma Membrane Redox Systems: Lipid Rafts and Protein Assemblies

Lüthje, Sabine

doi:10.1007/978-3-540-72954-9_7

Cited by 11 publications

(11 citation statements)

References 236 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The capability of plant cells to reduce external electron acceptors by means of a PM redox system is a long-known phenomenon with still scarce molecular basis (Lü thje, 2008). In whole cells or intact tissues, reduction of electron acceptors was found associated with apoplast acidification, membrane depolarization, or oxidation of internal electron donors, suggesting a transmembrane electron transfer chain fed by cytosolic reductants (Vuletić et al, 2005).…”

Section: Discussionmentioning

confidence: 99%

“…Trans-PM electron transport involving cytosolic NAD(P)H was also demonstrated, although it is not known whether a cytochrome was involved (Askerlund and Larsson, 1991;Menckhoff and Lü thje, 2004). In any case, because AIR12 is not a transmembrane protein, interactions with other redox partners would be needed to build up an electron route across the PM (Vuletić et al, 2005;Lü thje, 2008). Notably, only a few redox proteins known to interact with the PM are upregulated in Arabidopsis roots soon after auxin treatment and are implicated in lateral root emergence (Laskowski et al, 2006).…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Auxin-Responsive Genes AIR12 Code for a New Family of Plasma Membrane b-Type Cytochromes Specific to Flowering Plants

et al. 2009

View full text Add to dashboard Cite

We report here on the identification of the major plasma membrane (PM) ascorbate-reducible b-type cytochrome of bean (Phaseolus vulgaris) and soybean (Glycine max) hypocotyls as orthologs of Arabidopsis (Arabidopsis thaliana) AIR12 (for auxin induced in root cultures). Soybean AIR12, which is glycosylated and glycosylphosphatidylinositol-anchored to the external side of the PM in vivo, was expressed in Pichia pastoris in a recombinant form, lacking the glycosylphosphatidylinositol modification signal and purified from the culture medium. Recombinant AIR12 is a soluble protein predicted to fold into a b-sandwich domain and belonging to the DOMON (for dopamine b-monooxygenase N terminus) domain superfamily. It is shown to be a b-type cytochrome with a symmetrical a-band at 561 nm, fully reduced by ascorbate, and fully oxidized by monodehydroascorbate radical. AIR12 is a high-potential cytochrome b showing a wide bimodal dependence from the redox potential between +80 mV and +300 mV. Optical absorption and electron paramagnetic resonance analysis indicate that AIR12 binds a single, highly axial low-spin heme, likely coordinated by methionine-91 and histidine-76, which are strongly conserved in AIR12 sequences. Phylogenetic analyses reveal that the auxin-responsive genes AIR12 represent a new family of PM b-type cytochromes specific to flowering plants. Circumstantial evidence suggests that AIR12 may interact with other redox partners within the PM to constitute a redox link between cytoplasm and apoplast.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Auxin-Responsive Genes AIR12 Code for a New Family of Plasma Membrane b-Type Cytochromes Specific to Flowering Plants

et al. 2009

View full text Add to dashboard Cite

show abstract

“…For cell wall modification, the enzyme co-localized with Rboh (ruby colored) in microdomains. Simultaneously, superoxide dismutase (SOD, green) and ZmPrx01 regulate ROS levels at the PM [ 14 , 70 ]. ( c ) Soluble AtPrx64 interact with a transmembrane Casparian strip protein (CASP1, orange) at the PM [ 28 , 29 , 71 , 72 ].…”

Section: Figurementioning

confidence: 99%

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

Lüthje

Martínez-Cortés

2018

IJMS

Self Cite

View full text Add to dashboard Cite

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.

show abstract

“…The plasma membrane of plant cells displays transmembrane electron transport from cytoplasmic NAD(P)H to various external electron acceptors, which is accompanied by depolarization of the membrane potential and secretion of H 1 into the apoplast (Bérczi and Møller, 2000;Vuletić et al, 2005;Lü thje, 2007). Peculiar properties of this redox system, which can be demonstrated in right-side-out plasma membrane vesicles (Menckhoff and Lü thje, 2004), are as follows: (1) use of both NADH and NADPH as electron donors; (2) use of artificial substrates such as ferricyanide (FeCN), dichlorophenoleindophenole (DCPIP), or quinones as electron acceptors; and (3) insensitivity to KCN.…”

mentioning

confidence: 99%

Naphthoquinone-Dependent Generation of Superoxide Radicals by Quinone Reductase Isolated from the Plasma Membrane of Soybean

et al. 2008

View full text Add to dashboard Cite

Using a tetrazolium-based assay, a NAD(P)H oxidoreductase was purified from plasma membranes prepared from soybean (Glycine max) hypocotyls. The enzyme, a tetramer of 85 kD, produces O 2 Á2 by a reaction that depended on menadione or several other 1,4-naphthoquinones, in apparent agreement with a classification as a one-electron-transferring flavoenzyme producing semiquinone radicals. However, the enzyme displayed catalytic and molecular properties of obligatory two-electrontransferring quinone reductases of the DT-diaphorase type, including insensitivity to inhibition by diphenyleneiodonium. This apparent discrepancy was clarified by investigating the pH-dependent reactivity of menadionehydroquinone toward O 2 and identifying the protein by mass spectrometry and immunological techniques. The enzyme turned out to be a classical NAD(P)H:quinone-acceptor oxidoreductase (EC 1.6.5.2, formerly 1.6.99.2) that reduces menadione to menadionehydroquinone and subsequently undergoes autoxidation at pH $ 6.5. Autoxidation involves the production of the semiquinone as an intermediate, creating the conditions for one-electron reduction of O 2 . The possible function of this enzyme in the generation of O 2 Á2 and H 2 O 2 at the plasma membrane of plants in vivo is discussed.

show abstract

Plasma Membrane Redox Systems: Lipid Rafts and Protein Assemblies

Cited by 11 publications

References 236 publications

Auxin-Responsive Genes AIR12 Code for a New Family of Plasma Membrane b-Type Cytochromes Specific to Flowering Plants

Auxin-Responsive Genes AIR12 Code for a New Family of Plasma Membrane b-Type Cytochromes Specific to Flowering Plants

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

Naphthoquinone-Dependent Generation of Superoxide Radicals by Quinone Reductase Isolated from the Plasma Membrane of Soybean

Contact Info

Product

Resources

About