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Molecular Cloning and Ch.racterization of a Candidate ENOX Protein of <i>Sacch.romyces cerevisiae</i>with.a 25 Min Period Insensitive to Simalikalactone D Inh.bition and Melatonin

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Advances in Biological Ch.mistry 2014年第5期4卷 339-350页

作者： Aya F. Ryuzoji debby h. parisi Sara Dick James Kim Doroth. M. Morré D. James Morré Department of Biology Valparaiso University Valparaiso USA Mor-NuCo Inc. Purdue Research Park West Lafayette USA

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 exh.biting an oscillatory pattern with.a period length.of 25 min and resistant to th. ENOX1-specific inh.bitor simalikalactone D (YNOX for yeast-specific ENOX = ENOX4). Th. cDNA was cloned from a yeast over expression library using NADh.fluorescence analyzed by Fast Fourier transform and decomposition fits. Th. objective was to identify and sequence an ENOX h.mologue in Sacch.romyces cerevisiae with.a 25 min rath.r th.n a 24 min period length.(YNOX). Th. finding identified YDR005C as th. yeast ENOX protein with.a temperature-independent 25 min period length.and insensitive to inh.bition by simalikalactone D. Th. encoded protein was expressed in bacteria and ch.racterized. Gel slices corresponding to 55 kDa and 39 kDa h.s-tagged proteins exh.bited 25 min oscillatory patterns not inh.bited by 1 μM simalikalactone D for both.NADh.oxidation and reduced coenzyme Q10 oxidation as well as a protein disulfide-th.ol interch.nge activity wh.ch.alternated with.th. oxidative activities. Activities were ph.sed by low-frequency electromagnetic fields but, in contrast, to yeast ENOX1, not by addition of melatonin. Th. assay in th. presence of D2O sh.fted th. length.of th. oscillatory period from 25 min to 32 min. Th. YDR005C deletion mutant cells lacked th. ENOX4 clock output present in th. wild type yeast.

关键词： Biological Clock ECTO-NOX (ENOX) Proteins YNOX = ENOX4 Ultradian Oscillator Yeast (Sacch.romyces cerevisiae)

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Molecular cloning and ch.racterization of h.man age-related NADh.oxidase (arNOX) proteins as members of th. TM9 superfamily of transmembrane proteins

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Advances in Biological Ch.mistry 2013年第2期3卷 187-197页

作者： Xiaoyu Tang debby parisi Bradley Spicer Doroth. M. Morré D. James Morré Mor-NuCo Inc. Purdue Research Park West Lafayette USA

Age-related NADh.oxidase (arNOX = ENOX3) proteins are superoxide-generating cell surface oxidases th.t increase in activity with.age beginning at about 30 y. A soluble and truncated exfoliated form of th. activity is present in blood and oth.r body fluids. Th. activity was purified to apparent h.mogeneity from h.man urine and resolved by 2-D gel electroph.resis into a series of 24 to 32 kDa components of low isoelectric point. Th. purified proteins were resistant both.to N-terminal sequencing and trypsin cleavage. Cleavage with.pepsin revealed peptides corresponding to th. TM9 family of transmembrane proteins. Peptide antisera raised to all five members of th. h.man TM9 family sequentially blocked th. arNOX activity of h.man saliva and sera. Th. soluble truncated N-terminus of th. h.man h.molog TM9SF4 was expressed in bacteria. Th. recombinant protein was ch.racterized bioch.mically and exh.bited ar-NOX activity. Th. findings identify five arNOX isoforms each.of wh.ch.correspond to one of th. five known TM9 family members. Th. exfoliated soluble arNOX forms are derived from th. 24 to 32 kDa N-termini exposed to th. cell’s exterior at th. cell surface. Each.of th. sh.d forms contain putative functional motifs ch.racteristic of ECTO-NOX (ENOX) proteins despite only minimal sequence identity. Our findings identify arNOX as h.ving functional ch.racteristics of ENOX proteins and th. TM9 superfamily of proteins as th. genetic origins of th. five known arNOX isoforms present in h.man sera, plasma and oth.r body fluids1.

关键词： Age-Related NADh Oxidase (arNOX) TM-9 Superfamily of Transmembrane Proteins Molecular Cloning h.man Serum Plasma and Body Fluids Saliva

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