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PubMed2004

Nitrogen storage and its interaction with carbohydrates of young apple trees in response to nitrogen supply.

Bench-grafted 'Fuji/M.26' apple (Malus domestica Borkh.) trees received a constant nitrogen (N) supply (10.7 mM) from bud break to the end of June, and were then fertigated with 0, 5, 10, 15 or 20 mM N in a modified Hoagland's solution for 2 months during the summer. In mid-October, half of the trees fertigated at each N concentration were sprayed twice with 3% urea, whereas the remaining trees served as controls. All trees were harvested after natural leaf fall and were stored at 2 degrees C. Five trees from each of the N treatment combinations were destructively sampled during dormancy to determine the composition of N and total nonstructural carbohydrates (TNC). As the N supply from fertigation increased, amounts of N in both free amino acids and proteins increased, whereas C/N ratios decreased. Foliar urea applications in the fall significantly increased amounts of N in both free amino acids and proteins, but decreased their C/N ratios. Arginine, the most abundant amino acid in both free amino acids and in proteins, accounted for an increasing proportion of N in free amino acids and proteins with increasing N supply from fertigation or foliar urea application. The ratio of protein N to free amino acid N decreased from about 27.1 to 3.2 as N supply from fertigation increased from 0 to 20 mM, and decreased further to 3.0 in response to foliar urea applications in the fall. Concentrations of glucose, fructose, sucrose and TNC decreased as the N supply from fertigation increased, whereas concentrations of sorbitol and starch remained relatively unchanged. Foliar urea applications decreased the concentration of each TNC component and the TNC concentration in each N fertigation treatment. A negative linear relationship was found between carbon in TNC and N in proteins and free amino acids. The sum of carbon in TNC, proteins and free amino acids remained constant in response to N supply from fertigation. However, foliar urea applications decreased the sum of carbon in proteins, free amino acids and TNC because about 21% of the decrease in TNC carbon was not recovered in free amino acids or proteins. Young apple trees store N and carbon dynamically in response to N supply. As N supply increases, an increasing proportion of N is found in the form of free amino acids, which have a low carbon cost, although proteins remain the main form of N storage. Furthermore, part of the carbon from TNC is incorporated into amino acids and proteins, decreasing the carbon stored as TNC and increasing the carbon stored as amino acids and proteins.

Carbohydrate Metabolism↗

PubMed2003

The 50-kDa protein of Apple chlorotic leaf spot virus interferes with intracellular and intercellular targeting and tubule-inducing activity of the 39-kDa protein of Grapevine berry inner necrosis virus.

To understand why transgenic Nicotiana occidentalis plants expressing a functional movement protein (MP) of Apple chlorotic leaf spot virus (ACLSV) show specific resistance to Grapevine berry inner necrosis virus (GINV), the MPs of ACLSV (50KP) and GINV (39KP) were fused to green, yellow, or cyan fluorescent proteins (GFP, YFP, or CFP). These fusion proteins were transiently expressed in leaf cells of both transgenic (50KP) and nontransgenic (NT) plants, and the intracellular and intercellular trafficking and tubule-inducing activity of these proteins were compared. The results indicate that in epidermal cells and protoplasts from 50KP plant leaves, the trafficking and tubule-inducing activities of GINV-39KP were specifically blocked while those of ACLSV-50KP and Apple stem grooving virus MP (36KP) were not affected. Additionally, when 39KP-YFP and 50KP-CFP were coexpressed in the leaf epidermis of NT plants, the fluorescence of both proteins was confined to single cells, indicating that 50KP-CFP interferes with the cell-to-cell trafficking of 39KP-YFP and vice versa. Mutational analyses of 50KP showed that the deletion mutants that retained the activities described above still blocked cell-to-cell trafficking of 39KP, but the dysfunctional 50KP mutants could no longer impede cell-to-cell movement of 39KP. Transgenic plants expressing the functional 50KP deletion mutants showed specific resistance against GINV. In contrast, transgenic plants expressing the dysfunctional 50KP mutants did not show any resistance to the virus. From these results, we conclude that the specific resistance of 50KP plants to GINV is due to the ability of the 50KP to block intracellular and intercellular trafficking of GINV 39KP.

Gene Expression Regulation, Plant↗

PubMed1993

Striking similarities between the nucleotide sequence and genome organization of citrus tatter leaf and apple stem grooving capilloviruses.

The sequence of the 3'-terminal 2956 nucleotides, excluding the poly(A) tail, of the citrus tatter leaf virus (CTLV) genome was determined and compared with that of the apple stem grooving virus (ASGV) genome. The sequence of the 3'-terminal region of CTLV contains two overlapping open reading frames (ORFs) and a 3'-terminal non-coding region of 142 nucleotides. The long, incomplete ORF1 ends at UAG (position 2812) and encodes a protein with at least 938 amino acids (M(r) > 108,703). This protein contains the GDD motif associated with the RNA polymerase. ORF2, in a different frame within ORF1, starts at AUG (position 1248) and stops at UGA (position 2208) encoding a protein with an M(r) of 36,179 (36K). Partial homologies were found among the 36K protein of CTLV, the 50K protein of apple chlorotic leaf spot closterovirus, the 40K protein of potato virus T and the gene 1 products of caulimoviruses. The arrangement of ORFs in the 3'-terminal region of the CTLV genome is in perfect agreement with that of the ASGV genome. The sequence of the 3'-terminal 2956 nucleotides, excluding the poly(A) tail, of the CTLV genome shows 86.1% identity to that of the ASGV genome. Similarities of amino acid sequences encoded by ORF1 and ORF2 of CTLV with the corresponding regions of ASGV are 86.1% and 97.3%, respectively. These results indicate that CTLV is a capillovirus closely related to ASGV.

Amino Acid Sequence↗

PubMed2000

Nucleotide sequence and genome organization of apple latent spherical virus: a new virus classified into the family Comoviridae.

A virus with isometric virus particles (ca. 25 nm) was isolated from an apple tree and named Apple latent spherical virus (ALSV). Virus particles purified from infected Chenopodium quinoa formed two bands with densities of 1.41 and 1.43 g/cm(3) in CsCl equilibrium density-gradient centrifugation, indicating that the virus is composed of two components. The virus had two ssRNA species (RNA1 and RNA2) and three capsid proteins (Vp25, Vp24 and Vp20). The complete nucleotide sequences of RNA1 and RNA2 were determined to be 6815 nt and 3384 nt excluding the 3' poly(A) tail, respectively. RNA1 contains two partially overlapping ORFs encoding polypeptides of molecular mass 23 kDa ('23K'; ORF1) and 235 kDa ('235K'; ORF2); RNA2 has a single ORF encoding a polypeptide of 108 kDa ('108K'). The 235K protein has, in order, consensus motifs of the protease cofactor, the NTP-binding helicase, the cysteine protease and the RNA polymerase, in good agreement with the gene arrangement of viruses in the COMOVIRIDAE: The 108K protein contains an LPL movement protein (MP) motif near the N terminus. Direct sequencing of the N-terminal amino acids of the three capsid proteins showed that Vp25, Vp20 and Vp24 are located in this order in the C-terminal region of the 108K protein. The cleavage sites of the 108K polyprotein were Q/G (MP/Vp25 and Vp25/Vp20) and E/G (Vp20/Vp24). Phylogenetic analysis of the ALSV RNA polymerase domain showed that ALSV falls into a cluster different from the nepo-, como- and fabavirus lineages.

Amino Acid Sequence↗

PubMed2006

Erwinia tasmaniensis sp. nov., a non-phytopathogenic bacterium from apple and pear trees.

Bacteria were isolated from flowers and bark of apple and pear trees at three places in Australia. In Victoria, Tasmania and Queensland, strains with white colonies on nutrient agar were screened for dome-shaped colony morphology on agar with sucrose and were found to be closely related by several criteria. The isolates were not pathogenic on apples or pears. They were characterized by a polyphasic approach including microbiological and API assays as well as fatty acid methyl ester analysis, DNA-DNA hybridization and DNA sequencing. For molecular classification, the 16S rRNA cistron and the conserved genes gpd and recA of these bacteria were investigated. Together with other taxonomic criteria, the results of these studies indicate that the bacteria belong to a novel separate species, which we propose to name Erwinia tasmaniensis sp. nov., with the type strain Et1/99(T) (=DSM 17950(T)=NCPPB 4357(T)). From DNA-DNA hybridization kinetics, microbiological characteristics and nucleotide sequence analyses, this species is related to pathogenic Erwinia species, but also to the epiphytic species Erwinia billingiae.

Australia↗

PubMed2004

Evidence for apoplasmic phloem unloading in developing apple fruit.

The phloem unloading pathway remains unclear in fleshy fruits accumulating a high level of soluble sugars. A structural investigation in apple fruit (Malus domestica Borkh. cv Golden Delicious) showed that the sieve element-companion cell complex of the sepal bundles feeding the fruit flesh is symplasmically isolated over fruit development. 14C-autoradiography indicated that the phloem of the sepal bundles was functional for unloading. Confocal laser scanning microscopy imaging of carboxyfluorescein unloading showed that the dye remained confined to the phloem strands of the sepal bundles from the basal to the apical region of the fruit. A 52-kD putative monosaccharide transporter was immunolocalized predominantly in the plasma membrane of both the sieve elements and parenchyma cells and its amount increased during fruit development. A 90-kD plasma membrane H(+)-ATPase was also localized in the plasma membrane of the sieve element-companion cell complex. Studies of [14C]sorbitol unloading suggested that an energy-driven monosaccharide transporter may be functional in phloem unloading. These data provide clear evidence for an apoplasmic phloem unloading pathway in apple fruit and give information on the structural and molecular features involved in this process.

Biological Transport↗

PubMed1966

Purification and properties of apple fruit malic enzyme.

Malic enzyme was isolated and purified from mature apple fruits (Malus sylvestris, Miller) by utilizing procedures probably applicable to other soluble enzymes in this and similar tissues.The physical properties of apple fruit malic enzyme are similar to those reported for malic enzyme from other plant and animal sources. It is specific for l-malate, TPN and requires a divalent cation for activity. In contrast to the pigeon liver enzyme, supplemental TPN is not required for oxalacetic decarboxylase activity of the fruit enzyme. The pH optimum of the malic enzyme varied with the l-malate concentration and the nature of the divalent cation present. d-Malate activated the oxidation of l-malate at rate-limiting concentrations.

Journal Article↗

PubMed1966

Stimulation of ethylene production in apple tissue slices by methionine.

Methionine can induce more than a 100% increase in ethylene production by apple tissue slices. The increased amount of ethylene derives from carbons 3 and 4 of methionine. Only post-climacteric fruit tissues are stimulated by methionine, and stimulation is optimum after 8 months' storage. Copper chelators such as sodium diethyl dithiocarbamate and cuprizone very markedly inhibit ethylene production by tissue slices. Carbon monoxide does not effect ethylene production by the slices. These data suggest that the mechanism for the conversion of methionine to ethylene, in apple tissues, is similar to the previously described model system for producing ethylene from methionine and reduced copper. Therefore, it is suggested that one of the ethylene-forming systems in tissues derives from methionine and proceeds to ethylene via a copper enzyme system which may be a peroxidase.

Journal Article↗

PubMed1970

Calcium transport in apple trees.

(45)Ca, applied to roots of apple seedlings, moved readily to the developing leaves. Kinetin, benzyladenine, and B sprays increased movement. NO(3) (-) as the source of N increased movement and accumulation of Ca into mature leaves; NH(4) (+) increased movement into new leaves. Translocation in the stem is effected by a nonspecific ion exchange. Any divalent cation can free Ca for ascent. The exchange may be a property of lignin. Genetic differences in the uptake and translocation of Ca exist among apple seedlings. Those which show juvenile leaf characteristics translocate Ca into mature leaves more readily. Translocation of Ca in woody species appears to be similar to that reported for herbaceous plants.

Journal Article↗

PubMed1973

Flow of Chromium into Apple Fruit during Development.

A continuous flow of chromium into apples occurs throughout their growth. This ready movement of chromium into the apple is similar to that reported for essential trace elements such as boron, zinc, iron, copper, and manganese but differs from the restricted movement reported for mercury and cadmium.

Journal Article↗

PubMed1974

The occurrence and nature of ornithine carbamoyltransferase in senescing apple leaf tissue.

Ornithine carbamoyltransferase (EC 2.1.3.3) activity was detected in apple (Pyrus malus L.) leaf tissue from early June to November. Total activity remained relatively constant at 4.1 mumoles citrulline produced per hour per 10 cm(2) until mid-October when it sharply doubled. Following the first frost of the autumn, the enzyme lost about 80% of its former activity. The enzyme from apple leaf exhibited two pH optima, one at pH 8.6 and the other at pH 7.8, indicating the presence of isozymes or two forms of the enzyme. At pH 8.6, a partially-purified enzyme preparation had binding contrasts for its substrates of 6 mm for carbamyl-phosphate and 4.8 mm for ornithine. At pH 7.8, the Km for carbamyl-phosphate was 1.9 mm and the Km for ornithine was 1.22 mm.

Journal Article↗

PubMed1977

Localization of the Ethylene-synthesizing System in Apple Tissue.

Apple (Malus sp.) slices gradually lost the ability to synthesize ethylene when incubated with a mixture of enzymes that digest cell walls. The released protoplasts did not produce ethylene. The release of protoplasts was faster from climacteric fruit slices than from preclimacteric tissue. In protoplast suspension culture, as new cell wall was deposited (as judged by the intensity of fluorescence of regenerating protoplasts stained with Calcofluor White and the incorporation of labeled myo-inositol into their ethanol-insoluble residue), ethylene synthesis was gradually regained. Restored ethylene synthesis reached a maximum after 80 hours in protoplasts from preclimacteric fruit and in 120 hours in those from climacteric tissue. Addition of methionine (1 mm) to the culture medium was essential for appreciable synthesis of ethylene; and this synthesis was inhibited by the aminoethoxy analogue of rhizobitoxine and by propyl gallate, inhibitors of ethylene synthesis in higher plants. We suggest that the ethylene-synthesizing enzyme system is highly structured in the apple cell and is localized in a cell wall-cell membrane complex.

Journal Article↗

PubMed1977

Methionine metabolism in apple tissue: implication of s-adenosylmethionine as an intermediate in the conversion of methionine to ethylene.

If S-adenosylmethionine (SAM) is the direct precursor of ethylene as previously proposed, it is expected that 5'-S-methyl-5'-thioadenosine (MTA) would be the fragment nucleoside. When [Me-(14)C] or [(35)S]methionine was fed to climacteric apple (Malus sylvestris Mill) tissue, radioactive 5-S-methyl-5-thioribose (MTR) was identified as the predominant product and MTA as a minor one. When the conversion of methionine into ethylene was inhibited by (l)-2-amino-4-(2'-aminoethoxy)-trans-3-butenoic acid, the conversion of [(35)S] or [Me(14)C]methionine into MTR was similarly inhibited. Furthermore, the formation of MTA and MTR from [(35)S]methionine was observed only in climacteric tissue which produced ethylene and actively converted methionine to ethylene but not in preclimacteric tissue which did not produce ethylene or convert methionine to ethylene. These observations suggest that the conversion of methionine into MTA and MTR is closely related to ethylene biosynthesis and provide indirect evidence that SAM may be an intermediate in the conversion of methionine to ethylene.When [(35)S]MTA was fed to climacteric or preclimacteric apple tissue, radioactivity was efficiently incorporated into MTR and methionine. However, when [(35)S]MTR was administered, radioactivity was efficiently incorporated into methionine but not MTA. This suggests that the sulfur of MTA is incorporated into methionine via MTR. A dual label experiment with [(35)S, Me-(3)H]MTA indicates that the CH(3)S group of MTA was transferred as a unit to form methionine.A scheme is presented for the production of ethylene from methionine, the first step being the activation of methionine by ATP to give SAM. SAM is fragmented to give ethylene, MTA, and other products. MTA is then hydrolyzed to MTR which donates its methylthio group to a four-carbon acceptor to reform methionine.

Journal Article↗

PubMed1979

Detection and characterization of sorbitol dehydrogenase from apple callus tissue.

Sorbitol dehydrogenase (l-iditol:NAD(+) oxidoreductase, EC 1.1.1.14) has been detected and characterized from apple (Malus domestica cv. Granny Smith) mesocarp tissue cultures. The enzyme oxidized sorbitol, xylitol, l-arabitol, ribitol, and l-threitol in the presence of NAD. NADP could not replace NAD. Mannitol was slightly oxidized (8% of sorbitol). Other polyols that did not serve as substrate were galactitol, myo-inositol, d-arabitol, erythritol, and glycerol. The dehydrogenase oxidized NADH in the presence of d-fructose or l-sorbose. No detectable activity was observed with d-tagatose. NADPH could partially substitute for NADH.Maximum rate of NAD reduction in the presence of sorbitol occurred in tris(hydroxymethyl)aminomethane-HCl buffer (pH 9), or in 2-amino-2-methyl-1,3-propanediol buffer (pH 9.5). Maximum rates of NADH oxidation in the presence of fructose were observed between pH 5.7 and 7.0 with phosphate buffer. Reaction rates increased with increasing temperature up to 60 C. The K(m) for sorbitol and xylitol oxidation were 86 millimolar and 37 millimolar, respectively. The K(m) for fructose reduction was 1.5 molar.Sorbitol oxidation was completely inhibited by heavy metal ions, iodoacetate, p-chloromercuribenzoate, and cysteine. ZnSO(4) (0.25 millimolar) reversed the cysteine inhibition. It is suggested that apple sorbitol dehydrogenase contains sulfhydryl groups and requires a metal ion for full activity.

Journal Article↗

PubMed1981

Characterization and Partial Purification of Aldose-6-phosphate Reductase (Alditol-6-Phosphate:NADP 1-Oxidoreductase) from Apple Leaves.

Aldose-6-phosphate reductase (alditol 6-phosphate:NADP 1-oxidoreductase) was isolated and characterized from mature apple leaves (Malus domestica cv. Starkrimson). The enzyme was purified 79-fold. The enzyme catalyzed the following reversible reaction: d-glucose 6-phosphate + NADPH + H(+) right arrow over left arrow d-sorbitol 6-phosphate + NADP(+). No activity was detected when NAD(+) was substituted for NADP(+) or when NADH was substituted for NADPH. The enzyme reduced d-galactose 6-phosphate at a higher rate than d-glucose 6-phosphate. d-Mannose 6-phosphate and 2-deoxy-d-glucose 6-phosphate were reduced at low rates. d-Glucose 1-phosphate, d-fructose 6-phosphate, d-ribose 5-phosphate, d-glucose, and sorbitol did not serve as substrates. The pH optimum for both d-sorbitol 6-phosphate oxidation and d-glucose 6-phosphate reduction was 9.5. The K(m) values for d-sorbitol 6-phosphate oxidation and d-glucose 6-phosphate reduction were 3.9 and 20 millimolar, respectively. AgNO(3) (0.1 millimolar) and p-chloromercuribenzoate (1.0 millimolar) completely inhibited the enzyme.Aldose-6-phosphate reductase activity was also detected in mature leaves from Golden Delicious and Antonovka apples (Malus domestica), Conference and Bartlett pears (Pyrus communis), Redhaven peach (Prunus persica), and Perfection apricot (Prunus armeniaca). This suggests that the enzyme has a wide distribution and plays an important role in sorbitol synthesis.

Journal Article↗

PubMed1982

Sorbitol metabolism and sink-source interconversions in developing apple leaves.

In apple (Malus domestica Borkh.) sorbitol is the primary product of photosynthesis, the major translocated form of carbon, and a common fruit constituent and storage compound. Previous work on sorbitol metabolism has revealed a NADPH-dependent aldose 6-phosphate reductase (A6PR) in green tissues, and a NAD-dependent sorbitol dehydrogenase in nongreen tissues. Results here show a decrease in sorbitol dehydrogenase activity and an increase in A6PR activity as leaves developing in the spring undergo the transition from sink to source. Sorbitol dehydrogenase activity reached a minimum as A6PR peaked. These changes were related to increases in leaf carbohydrate levels, especially sorbitol, and to increases in rates of net photosynthesis. Studies conducted in the autumn on senescing leaves also showed changes in enzyme activites, leaf carbohydrate levels, and photosynthesis. At this time, however, sorbitol dehydrogenase increased in specific activity, whereas A6PR activity, leaf carbohydrates, and photosynthetic rates all decreased substantially. Other experiments showed differences in the ability of young and mature leaves to metabolize sorbitol and in the distribution of sorbitol enzymes in leaves at transitional developmental stages. The results suggest that sorbitol metabolism in apple is tightly controlled and may be related to mechanisms regulating partitioning or source and sink activity.

Journal Article↗

PubMed1982

Characteristics and Activity Changes of Proteolytic Enzymes in Apple Leaves during Autumnal Senescence.

At least four different proteinases are present in senescing apple leaves (Malus domestica Borkh. cv. Golden Delicious) as determined by their pH optima, substrate specificity, and their reactivity to proteinase inhibitors. An enzyme active at pH 4.5 to 5.0 appears to be a sulfhydryl-dependent (iodoacetamide and phenylmercuric acetate-sensitive) endoproteinase, and degradation of the large subunit of ribulose bisphosphate carboxylase was observed only with this enzyme. It is tentatively concluded that this endoproteinase is responsible for the breakdown of ribulose bisphosphate carboxylase in vivo. However, the presence of more than one endoproteinase in apple leaves is suggested by the broad range of pH optima of the SH-dependent enzyme. Another enzyme active at pH 6.0 appears to be a carboxypeptidase, and was sensitive to phenylmethylsulfonylfluoride. This enzyme showed a strong hydrolytic activity against carbobenzoxyphenylalanylalanine. A sulfhydryl-dependent aminopeptidase and a second hydroxyl-dependent carboxypeptidase were active at pH 7.5Total autolytic activity (the sulfhydryl-dependent endoproteinase) as measured by the disappearance of proteins decreased during the period of protein decline. Evidence is presented that the measured proteinase activity can be dependent on assay methods and substrates. While the disappearance of protein measures most of endo-type activity, the ninhydrin assay appears to measure exo-type activity preferentially.

Journal Article↗

PubMed1985

Proteins and peroxidase in callus and suspension cultures of apple : a study using ultrathin-layer isoelectric focusing, sensitive silver staining of proteins, and peroxidase isozyme visualization.

Different methods for the isolation of soluble proteins were applied to cell cultures of three apple cultivars (Malus sylvestris Mill.), best results being obtained with a rapid technique based on freezing and thawing. Ultrathin-layer isoelectric focusing followed by an improved silver staining method has shown that proteins from apple callus cultures consist of some 60 to 80 zones, with isoelectric points mainly between pH 4 to 7. Depending on protein content, adequate silver staining is achieved with 50 to 500 cells. Protein patterns of callus cultures allowed clear discrimination of cultivars. Protein and peroxidase isozyme patterns in cell saps of suspension cultures show striking differences during the growth cycle, whereas the protein patterns from the nutrient media were constant over the entire cultivation period and closely resembled the patterns of stationary phase and callus cells.

Journal Article↗