Disease relevance of Prunus

• In the present work we have studied the accumulation of gentisic acid (2,5-dihydroxybenzoic acid, a metabolic derivative of salicylic acid, SA) in the plant-pathogen systems, Cucumis sativus and Gynura aurantiaca, infected with either prunus necrotic ringspot virus (PNRSV) or the exocortis viroid (CEVd), respectively [1].
• Improvement of hyperglycemia and hyperlipemia in streptozotocin-diabetic rats by a methanolic extract of Prunus davidiana stems and its main component, prunin [2].
• Sour cherry (Prunus cerasus L.) scion cv. Montmorency and rootstock cv. Gisela 6 (P. cerasus x P. canescens) were transformed using Agrobacterium tumefaciens strain EHA105:pBISN1 carrying the neomycin phosphotransferase gene (nptII) and an intron interrupted ss-glucuronidase (GUS) reporter gene (gusA) [3].
• Toxicity studies were conducted on Brassica rapa, Prunus amygdalus and Zingiber officinale, used as aphrodisiacs in Arab Medicine. During acute toxicity test observations were made for 24 h where all these plants showed no toxicity [4].

High impact information on Prunus

• Recently, an S haplotype-specific F-box (SFB) gene has been proposed as a candidate for the pollen-S specificity gene of RNase-mediated gametophytic self-incompatibility in Prunus (Rosaceae) [5].
• Interestingly, LuHNL like ADH and Prunus serotina (PsHNL) possesses an ADP-binding betaalphabeta unit motif, pointing to the possibility that the non-flavoprotein PsHNL and the flavoprotein LuHNL have developed from two independent lines of evolution of a common ancestor with an ADP-binding betaalphabeta unit [6].
• QRT3 encodes a protein that is approximately 30% similar to an endopolygalacturonase from peach (Prunus persica) [7].
• To understand key steps in long-distance transport and particularly partitioning and accumulation of sorbitol in sink tissues, we have cloned two sorbitol transporter genes (PcSOT1 and PcSOT2) from sour cherry (Prunus cerasus) fruit tissues that accumulate large quantities of sorbitol [8].
• In black cherry (Prunus serotina Ehrh.) seed homogenates, (R)-amygdalin is degraded to HCN, benzaldehyde, and glucose by the sequential action of amygdalin hydrolase (AH), prunasin hydrolase (PH), and mandelonitrile lyase [9].

Chemical compound and disease context of Prunus

• We constructed a gene library of a nopaline-type Ti plasmid (called pTi-SAKURA) which was newly isolated from Agrobacterium tumefaciens MAFF301001 of a Japanese cherry tree [10].

Biological context of Prunus

• Three forms of prunasin hydrolase (PH I, PH IIa, and PH IIb), which catalyze the hydrolysis of (R)-prunasin to mandelonitrile and D-glucose, have been purified from homogenates of mature black cherry (Prunus serotina Ehrh.) seeds [11].
• A cDNA for an S-like RNase (RNase PD2) has been isolated from a pistil cDNA library of Prunus dulcis cv. Ferragnés. The cDNA encodes an acidic protein of 226 amino acid residues with a molecular weight of 25 kDa [12].
• Ethylene-responsive genes are differentially regulated during abscission, organ senescence and wounding in peach (Prunus persica) [13].
• Complete amino acid sequence determination of the major allergen of peach (Prunus persica) Pru p 1 [14].
• A genomic DNA sequence (PpACO1) encoding 1-aminocyclopropane-1-carboxylic acid oxidase (ACO) from peach (Prunus persica L. Batsch cv. Loring) was isolated [15].

Associations of Prunus with chemical compounds

• The major allergen of peach (Prunus persica) is a lipid transfer protein [16].
• In black cherry (Prunus serotina Ehrh.) macerates, the cyanogenic diglucoside (R)-amygdalin undergoes stepwise degradation to HCN catalyzed by amygdalin hydrolase (AH), prunasin hydrolase, and (R)-(+)-mandelonitrile lyase (MDL) [17].
• A 2.2 kb transcript accumulated in ethylene activated abscission zones of leaves and fruits, and ppEG1 (Prunus persica endoglucanase 1) the gene coding for pCel 10, was isolated and characterized [18].
• The deduced protein sequence of GhGLP1 is similar to Prunus persica auxin-binding proteins, a barley ADP-glucose pyrophosphatase/phosphodiesterase and two different classes of hydrogen peroxide-producing enzymes: wheat germin oxalate oxidase and moss extracellular Mn-superoxide dismutase [19].
• The FAD-dependent hydroxynitrile lyase from almond (Prunus amygdalus, PaHNL) catalyzes the cleavage of R-mandelonitrile into benzaldehyde and hydrocyanic acid [20].

Gene context of Prunus

• Two distinct partial cDNAs, PRF1 and PRF3, similar in sequence to previously described polygalacturonases, were amplified from ripe peach (Prunus persica L. Batsch cv Flavorcrest) fruit cDNA by the polymerase chain reaction [21].
• In contrast, RcOMT2, which shows 94% similarity with caffeic acid O-methyltransferase (COMT) of Prunus amygdalus, was expressed in all tissues tested and had the highest activity with caffeic acid, a typical substrate for COMT [22].
• The sequence of an alpha-tubulin from Prunus amygdalus has been obtained by cDNA cloning [23].
• The cDNA, designated Pa-RRM-GRP1 (Prunus avium RNA recognition motif glycine-rich protein 1), contains a single N-terminal RNA recognition motif (RRM) and single C-terminal glycine-rich domain [24].
• To identify which processes in peach, Prunus persica [L.] Batsch., are associated with changes in ethylene perception, we cloned and characterized a peach homologue of the gene encoding the ethylene receptor, ETR1 [25].

Analytical, diagnostic and therapeutic context of Prunus

• Molecular cloning and biochemical characterization of a lipoxygenase in almond (Prunus dulcis) seed [26].
• To obtain a candidate auxin-binding protein (ABP), a soluble 60 kDa protein was isolated from an extract of shoot apices of peach trees (Prunus persica L.) by affinity chromatography on a 2,4-dichlorophenoxyacetic acid (2,4-D)-linked Sepharose4B column [27].
• Northern blotting and RT-PCR analyses indicate that PD2 is expressed predominantly in petals, pistils of open flowers and leaves of the almond tree [12].
• Authenticity assessment of gamma- and delta-decalactone from prunus fruits by gas chromatography combustion/pyrolysis isotope ratio mass spectrometry (GC-C/P-IRMS) [28].
• An aminopeptidase was purified about 1,700-fold from seeds of Japanese apricot (Prunus mume Sieb.) by a seven-step procedure comprising extraction from seeds, ammonium sulfate fractionation, DEAE-cellulose chromatography, first and second DEAE-Sepharose chromatography, hydroxyapatite chromatography, and Sephadex G-200 gel filtration [29].

References