NADH Oxidase: A Multifunctional Ectoprotein of the Eukaryotic Cell Surface

Morré, D. James

doi:10.1007/978-94-017-2695-5_5

Cited by 76 publications

(64 citation statements)

References 106 publications

(65 reference statements)

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“…In addition to NADH oxidation, both activities catalyze hydroquinone oxidation and protein disulfide-thiol interchange as evidenced by cleavage of the dithio-dipyridine (DTDP) substrate. These activities, NADH or hydroquinone oxidation and protein disulfide-thiol interchange, alternate in a manner unprecedented in the biochemical literature and are unique to the ENOX family of proteins [1] [12].…”

Section: Discussionmentioning

confidence: 99%

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Molecular Cloning and Characterization of a Candidate ENOX Protein of Saccharomyces cerevisiae with a 25 Min Period Insensitive to Simalikalactone D Inhibition and Melatonin

Ryuzoji¹,

Parisi²,

Dick³

et al. 2014

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A yeast deletion library was screened based on NADH fluorescence using a 384-well plate assay to identify a yeast isolate lacking a previously identified cell surface oxidase exhibiting an oscillatory pattern with a period length of 25 min and resistant to the ENOX1-specific inhibitor simalikalactone D (YNOX for yeast-specific ENOX = ENOX4). The cDNA was cloned from a yeast over expression library using NADH fluorescence analyzed by Fast Fourier transform and decomposition fits. The objective was to identify and sequence an ENOX homologue in Saccharomyces cerevisiae with a 25 min rather than a 24 min period length (YNOX). The finding identified YDR005C as the yeast ENOX protein with a temperature-independent 25 min period length and insensitive to inhibition by simalikalactone D. The encoded protein was expressed in bacteria and characterized. Gel slices corresponding to 55 kDa and 39 kDa His-tagged proteins exhibited 25 min oscillatory patterns not inhibited by 1 µM simalikalactone D for both NADH oxidation and reduced coenzyme Q10 oxidation as well as a protein disulfide-thiol interchange activity which alternated with the oxidative activities. Activities were phased by low-frequency electromagnetic fields but, in contrast, to yeast ENOX1, not by addition of melatonin. The assay in the presence of D 2 O shifted the length of the oscillatory period from 25 min to 32 min. The YDR005C deletion mutant cells lacked the ENOX4 clock output present in the wild type yeast.

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Section: Discussionmentioning

confidence: 99%

“…They are protease and heat resistant [22] and responsive to hormones and growth factors [1] [23]. The constitutive ENOX1 serves as an ultradian oscillator of the biological clock [14] and, as such, is important for understanding circadian rhythms.…”

Section: Discussionmentioning

confidence: 99%

Molecular Cloning and Characterization of a Candidate ENOX Protein of Saccharomyces cerevisiae with a 25 Min Period Insensitive to Simalikalactone D Inhibition and Melatonin

Ryuzoji¹,

Parisi²,

Dick³

et al. 2014

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“…Hormone-responsive NADH oxidase activity has been detected in both plant and animal PM and identified as NADH oxidase (or NOX) enzymes. To distinguish the plant enzyme from the other enzymes the name dNOX was introduced [referring to its 2,4-dichlorophenoxyacetic acid (2,4-D) stimulation; Morré 1998b]. Recently, a new protocol was introduced for the purification of dNOX (Morré & Morré 1998), which significantly differed from the protocol published earlier.…”

Section: Nadh Oxidasesmentioning

confidence: 99%

Redox enzymes in the plant plasma membrane and their possible roles

Bérczi

Møller

2000

Plant Cell & Environment

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“…A distinguishing characteristic of ENOX proteins that permits their unequivocal identification is that the proteins exhibit two activities that alternate [1]- [3]. The first activity is that of a hydroquinone oxidase (NADH serves as an alternate substrate for this activity) [23].…”

Section: Introductionmentioning

confidence: 99%

“…One or more hormone-responsive external plasma membrane hydroquinone oxidases capable of catalyzing protein disulfide interchange and that oxidize NAD(P)H as an alternate substrate (External NADH oxidase = ENOX) have been exhibited by all animal and plant species, thus far investigated, as well as by yeast [1]- [3]. Based on activity characteristics, three related ENOX proteins have emerged.…”

Section: Introductionmentioning

confidence: 99%

Molecular Cloning and Characterization of a Candidate Plant Growth-Related and Time-Keeping Constitutive Cell Surface Hydroquinone (NADH) Oxidase (ENOX1) from Arabidopsis lyrata

Tang¹,

Ades²,

Morré³

et al. 2015

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ENOX (ECTO-NOX) proteins are proteins of the external surface of the plasma membrane that catalyze oxidation of both NADH and hydroquinones as well as carry out protein disulfide-thiol interchange. They exhibit both prion-like and time-keeping (clock) properties. The oxidative and interchange activities alternate to generate a regular period of 24 min in length. Here we report the cloning, expression, and characterization of a plant candidate constitutive ENOX (CNOX or ENOX1) protein from Arabidopsis lyrata. The gene encoding the 335 (165) amino acid protein is found in accession XP-002882467. Functional motifs characteristics of ENOX proteins previously identified by site-directed mutagenesis and present in the candidate ENOX1 protein from plants include adenine nucleotide and copper binding motifs along with essential cysteines. However, the drug binding motif (EEMTE) sequence of human ENOX2 is absent. The activities of the recombinant protein expressed in E. coli were unaffected by capsaicin, EGCg, and other ENOX2-inhibiting substances. Periodic oxidative activity was exhibited both with NAD(P)H and reduced coenzyme Q as substrate. Bound copper was necessary for activity and activity was inhibited by the ENOX1-specific inhibitor simalikalactone D. Addition of melatonin phased the 24-min period such that the next complete period began 24 min after the melatonin addition as appeared to be characteristic of ENOX1 activities in general. Periodic protein disulfide-thiol interchange activity also was demonstrated along with the 2 oxidative plus 3 interchange activity pattern characteristics of the 24-min ENOX1 protein period. Concentrated solutions of the purified plant ENOX1 protein formed insoluble aggregates, devoid of enzymatic activity, resembling amyloid. Activity was restored to * Corresponding author. X. Y. Tang et al.2 aggregate preparations by isoelectric focusing.

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NADH Oxidase: A Multifunctional Ectoprotein of the Eukaryotic Cell Surface

Cited by 76 publications

References 106 publications

Molecular Cloning and Characterization of a Candidate ENOX Protein of <i>Saccharomyces cerevisiae</i> with a 25 Min Period Insensitive to Simalikalactone D Inhibition and Melatonin

Molecular Cloning and Characterization of a Candidate ENOX Protein of <i>Saccharomyces cerevisiae</i> with a 25 Min Period Insensitive to Simalikalactone D Inhibition and Melatonin

Redox enzymes in the plant plasma membrane and their possible roles

Molecular Cloning and Characterization of a Candidate Plant Growth-Related and Time-Keeping Constitutive Cell Surface Hydroquinone (NADH) Oxidase (ENOX1) from <i>Arabidopsis lyrata</i>

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NADH Oxidase: A Multifunctional Ectoprotein of the Eukaryotic Cell Surface

Cited by 76 publications

References 106 publications

Molecular Cloning and Characterization of a Candidate ENOX Protein of &lt;i&gt;Saccharomyces cerevisiae&lt;/i&gt; with a 25 Min Period Insensitive to Simalikalactone D Inhibition and Melatonin

Molecular Cloning and Characterization of a Candidate ENOX Protein of &lt;i&gt;Saccharomyces cerevisiae&lt;/i&gt; with a 25 Min Period Insensitive to Simalikalactone D Inhibition and Melatonin

Redox enzymes in the plant plasma membrane and their possible roles

Molecular Cloning and Characterization of a Candidate Plant Growth-Related and Time-Keeping Constitutive Cell Surface Hydroquinone (NADH) Oxidase (ENOX1) from &lt;i&gt;Arabidopsis lyrata&lt;/i&gt;

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Molecular Cloning and Characterization of a Candidate ENOX Protein of <i>Saccharomyces cerevisiae</i> with a 25 Min Period Insensitive to Simalikalactone D Inhibition and Melatonin

Molecular Cloning and Characterization of a Candidate ENOX Protein of <i>Saccharomyces cerevisiae</i> with a 25 Min Period Insensitive to Simalikalactone D Inhibition and Melatonin

Molecular Cloning and Characterization of a Candidate Plant Growth-Related and Time-Keeping Constitutive Cell Surface Hydroquinone (NADH) Oxidase (ENOX1) from <i>Arabidopsis lyrata</i>