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Sheng Wu Gong Cheng Xue Bao = Chinese... Jan 2018Aphids are major agricultural pests that cause significant yield losses of crops each year. (E)-β-farnesene (EβF), as the main component of the aphid alarm pheromones,... (Review)
Review
Aphids are major agricultural pests that cause significant yield losses of crops each year. (E)-β-farnesene (EβF), as the main component of the aphid alarm pheromones, can interrupt aphid feeding and cause other conspecies in the vicinity to become agitated or disperse from their host plant. Furthermore, EβF can function as a kairomone in attracting aphid predators. EβF synthase genes, which encode enzymes that convert farnesyl diphosphate (FPP) to the acyclic sesquiterpene EβF, have been isolated and characterized from peppermint (Mentha × piperita and Mentha asiatica), Yuzu (Citrus junos), Douglas fir (Pseudotsuga menziesii), sweet wormwood (Artemisia annua) and chamomile (Matricaria recutita), respectively. Transgenic plant overexpressing EβF synthase genes has been one of the most efficient strategies for aphid management. In this review, the current statuses of transgenic plants engineered for aphid resistance were summarized. The plant-derived EβF synthase genes with their potential roles in aphid management via genetic-modified (GM) approaches were reviewed. The existing problem in GM plants with EβF synthase gene, such as low EβF emission was usually detected in the transgenic plant, was discussed and the development direction in this area was proposed.
Topics: Animals; Aphids; Metabolic Engineering; Plants, Genetically Modified; Pyrophosphatases; Sesquiterpenes
PubMed: 29380567
DOI: 10.13345/j.cjb.170093 -
International Journal of Developmental... Feb 2018There is growing evidence that over consumption of high-fat foods and insulin resistance may alter hippocampal-dependent cognitive function. To study the individual... (Review)
Review
There is growing evidence that over consumption of high-fat foods and insulin resistance may alter hippocampal-dependent cognitive function. To study the individual contributions of diet and peripheral insulin resistance to learning and memory, we used a transgenic mouse line that overexpresses ecto-nucleotide pyrophosphatase phosphodiesterase-1 in adipocytes, which inhibits the insulin receptor. Here, we demonstrate that a model of peripheral insulin resistance exacerbates high-fat diet induced deficits in performance on the Morris Water Maze task. This finding was then reviewed in the context of the greater literature to explore potential mechanisms including triglyceride storage, adiponectin, lipid composition, insulin signaling, oxidative stress, and hippocampal signaling. Together, these findings further our understanding of the complex relationship among peripheral insulin resistance, diet and memory.
Topics: Animals; Brain; Cognition Disorders; Diet, High-Fat; Insulin Resistance; Mice; Mice, Transgenic; Oxidative Stress; Phosphoric Diester Hydrolases; Pyrophosphatases
PubMed: 28373023
DOI: 10.1016/j.ijdevneu.2017.03.011 -
The FEBS Journal Sep 2016ADP-ribosylation is a conserved post-translational protein modification that plays a role in all major cellular processes, particularly DNA repair, transcription,...
ADP-ribosylation is a conserved post-translational protein modification that plays a role in all major cellular processes, particularly DNA repair, transcription, translation, stress response and cell death. Hence, dysregulation of ADP-ribosylation is linked to the physiopathology of several human diseases including cancers, diabetes and neurodegenerative disorders. Protein ADP-ribosylation can be reversed by the macrodomain-containing proteins PARG, TARG1, MacroD1 and MacroD2, which hydrolyse the ester bond known to link proteins to ADP-ribose as well as consecutive ADP-ribose subunits; targeting this bond can thus result in the complete removal of the protein modification or the conversion of poly(ADP-ribose) to mono(ADP-ribose). Recently, proteins containing the NUDIX domain - namely human NUDT16 and bacterial RppH - have been shown to process in vitro protein ADP-ribosylation through an alternative mechanism, converting it into protein-conjugated ribose-5'-phosphate (R5P, also known as pR). Though this protein modification was recently identified in mammalian tissues, its physiological relevance and the mechanism of generating protein phosphoribosylation are currently unknown. Here, we identified ectonucleotide pyrophosphatase/phosphodiesterase 1 (ENPP1) as the first known mammalian enzyme lacking a NUDIX domain to generate pR from ADP-ribose on modified proteins in vitro. Thus, our data show that at least two enzyme families - Nudix and ENPP/NPP - are able to metabolize protein-conjugated ADP-ribose to pR in vitro, suggesting that pR exists and may be conserved from bacteria to mammals. We also demonstrate the utility of ENPP1 for converting protein-conjugated mono(ADP-ribose) and poly(ADP-ribose) into mass spectrometry-friendly pR tags, thus facilitating the identification of ADP-ribosylation sites.
Topics: ADP Ribose Transferases; Adenosine Diphosphate Ribose; Amino Acid Sequence; Animals; Binding Sites; Humans; In Vitro Techniques; Mice; Phosphoric Diester Hydrolases; Poly (ADP-Ribose) Polymerase-1; Poly(ADP-ribose) Polymerases; Protein Domains; Protein Processing, Post-Translational; Proto-Oncogene Proteins; Pyrophosphatases; Recombinant Proteins; Sequence Homology, Amino Acid; Tandem Mass Spectrometry
PubMed: 27406238
DOI: 10.1111/febs.13811 -
Protein Science : a Publication of the... Oct 2020The ecto-nucleoside triphosphate diphosphohydrolases (NTPDases) are a family of enzymes found on the cell surface and in the lumen of certain organelles, that are major...
The ecto-nucleoside triphosphate diphosphohydrolases (NTPDases) are a family of enzymes found on the cell surface and in the lumen of certain organelles, that are major regulators of purinergic signaling. Their intracellular roles, however, have not been clearly defined. NTPDase4 (UDPase, ENTPD4) is a Golgi protein potentially involved in nucleotide recycling as part of protein glycosylation, and is also found in lysosomes, where its purpose is unknown. To further our understanding of NTPDase4 function, we determined its crystal structure. The enzyme adopts a wide open, inactive conformation. Differences in the nucleotide-binding site relative to its homologs could account for its substrate selectivity. The putative membrane-interacting loop of cell-surface NTPDases is drastically altered in NTPDase4, potentially affecting its interdomain dynamics at the Golgi membrane.
Topics: Animals; Crystallography, X-Ray; Humans; Protein Domains; Protein Structure, Secondary; Pyrophosphatases; Sf9 Cells; Spodoptera
PubMed: 32767432
DOI: 10.1002/pro.3926 -
The Journal of Investigative Dermatology May 2021In the past two decades, there has been great progress in identifying the molecular basis and pathomechanistic details in pseudoxanthoma elasticum (PXE), a heritable... (Review)
Review
In the past two decades, there has been great progress in identifying the molecular basis and pathomechanistic details in pseudoxanthoma elasticum (PXE), a heritable multisystem ectopic mineralization disorder. Although the identification of pathogenic variants in ABCC6 has been critical for understanding the disease process, genetic modifiers have been disclosed that explain the phenotypic heterogeneity of PXE. Adding to the genetic complexity of PXE are PXE-like phenotypes caused by pathogenic variants in other ectopic mineralization-associated genes. This review summarizes the current knowledge of the genetics and candidate modifier genes in PXE, a multifactorial disease at the genome-environment interface.
Topics: Animals; Diphosphates; Genetic Association Studies; Humans; Mice; Multidrug Resistance-Associated Proteins; Oxidative Stress; Phosphoric Diester Hydrolases; Pseudoxanthoma Elasticum; Pyrophosphatases; Vascular Calcification
PubMed: 33341249
DOI: 10.1016/j.jid.2020.10.013 -
The Plant Cell May 2018
Topics: Arabidopsis; Diphosphates; Inorganic Pyrophosphatase; Pyrophosphatases; Vacuoles
PubMed: 29716989
DOI: 10.1105/tpc.18.00342 -
Clinical Pharmacology and Therapeutics May 2019
Topics: Alleles; Biotransformation; Cytochrome P-450 Enzyme System; Genome-Wide Association Study; Haplotypes; Humans; Medication Therapy Management; Pharmacogenetics; Pharmacogenomic Testing; Pharmacogenomic Variants; Pyrophosphatases; Terminology as Topic
PubMed: 30515762
DOI: 10.1002/cpt.1268 -
PLoS Pathogens Aug 2016
Review
Topics: Host-Pathogen Interactions; Plant Diseases; Plant Immunity; Plants; Pyrophosphatases; Nudix Hydrolases
PubMed: 27513453
DOI: 10.1371/journal.ppat.1005704 -
Acta Crystallographica. Section F,... Nov 2018Ectonucleotide phosphodiesterase/pyrophosphatase-3 (NPP3, ENPP3) is an ATP-hydrolyzing glycoprotein that is located in the extracellular space. The full-length...
Ectonucleotide phosphodiesterase/pyrophosphatase-3 (NPP3, ENPP3) is an ATP-hydrolyzing glycoprotein that is located in the extracellular space. The full-length ectodomain of rat NPP3 was expressed in HEK293S GntI cells, purified using two chromatographic steps and crystallized. Its structure at 2.77 Å resolution reveals that the active-site zinc ions are missing and a large part of the active site and the surrounding residues are flexible. The SMB-like domains have the same orientation in all four molecules in the asymmetric unit. The SMB2 domain is oriented as in NPP2, but the SMB1 domain does not interact with the PDE domain but extends further away from the PDE domain. Deletion of the SMB domains resulted in crystals that diffracted to 2.4 Å resolution and are suitable for substrate-binding studies.
Topics: Binding Sites; Catalytic Domain; Crystallization; Crystallography, X-Ray; HEK293 Cells; Humans; Phosphoric Diester Hydrolases; Protein Domains; Pyrophosphatases; Recombinant Proteins; Somatomedins
PubMed: 30387774
DOI: 10.1107/S2053230X18011111 -
Scientific Reports Dec 2015ADP-ribosylation refers to the transfer of the ADP-ribose group from NAD(+) to target proteins post-translationally, either attached singly as mono(ADP-ribose) (MAR) or...
ADP-ribosylation refers to the transfer of the ADP-ribose group from NAD(+) to target proteins post-translationally, either attached singly as mono(ADP-ribose) (MAR) or in polymeric chains as poly(ADP-ribose) (PAR). Though ADP-ribosylation is therapeutically important, investigation of this protein modification has been limited by a lack of proteomic tools for site identification. Recent work has demonstrated the potential of a tag-based pipeline in which MAR/PAR is hydrolyzed down to phosphoribose, leaving a 212 Dalton tag at the modification site. While the pipeline has been proven effective by multiple groups, a barrier to application has become evident: the enzyme used to transform MAR/PAR into phosphoribose must be purified from the rattlesnake Crotalus adamanteus venom, which is contaminated with proteases detrimental for proteomic applications. Here, we outline the steps necessary to purify snake venom phosphodiesterase I (SVP) and describe two alternatives to SVP-the bacterial Nudix hydrolase EcRppH and human HsNudT16. Importantly, expression and purification schemes for these Nudix enzymes have already been proven, with high-quality yields easily attainable. We demonstrate their utility in identifying ADP-ribosylation sites on Poly(ADP-ribose) Polymerase 1 (PARP1) with mass spectrometry and discuss a structure-based rationale for this Nudix subclass in degrading protein-conjugated ADP-ribose, including both MAR and PAR.
Topics: Adenosine Diphosphate Ribose; Animals; Bacterial Proteins; Crotalid Venoms; Humans; Phosphodiesterase I; Proteomics; Pyrophosphatases; Viperidae; Nudix Hydrolases
PubMed: 26669448
DOI: 10.1038/srep18271