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Plant Physiol. 1993 Jan;101(1):201-208.
Abolition of an Inducible Highly Anionic Peroxidase Activity in Transgenic Tomato.

Sherf BA, Bajar AM, Kolattukudy PE.

The Ohio State Biotechnology Center, 1060 Carmack Road, Columbus, Ohio 43210.

Locally induced expression of a highly anionic peroxidase has previously been correlated temporally and spatially with suberization of tissues responding to pathogen assault, wounding, or exogenously applied abscisic acid or fungal elicitors. DNA sequences corresponding to the 5[prime] regions of two tomato (Lycopersicon esculentum) genes encoding homologous anionic peroxidases were fused, inserted into a pTi-based plasmid designed to express a composite antisense transcript, and introduced into tomato via Agrobacterium-mediated transformation. RNA gel-blot analyses showed high expression of the antisense transcript in most transgenic plants and no detectable induction of native anionic peroxidase transcripts in wounded or abscisic acid or pathogen-treated tissues. Plants and fruits expressing the antisense transcript appeared normal in all respects. Electrophoretic analysis of anionic proteins from selected transgenic plants showed no detectable anionic peroxidase protein or activity. Depolymerization of polymeric material from the wound periderm of transgenic tomato fruits and analysis of the aliphatic products by gas-liquid chromatography/mass spectrometry showed that the content and composition of C16/C18 [omega]-hydroxy and dicarboxylic acids, characteristic of suberin, were not affected by the absence of the anionic peroxidase. Autofluorescence generated from cell wall phenolics at the wound lesion was also not affected by the absence of the highly anionic peroxidase.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12231677&dopt=Abstract [PubMed - as supplied by publisher]

Plant Physiol. 1993 Jan;101(1):297-301.
Stimulation of Barley Plasmalemma H+-ATPase by Phytotoxic Peptides from the Fungal Pathogen Rhynchosporium secalis.

Wevelsiep L, Rupping E, Knogge W.

Max-Planck-Institut fur Zuchtungsforschung, Department of Biochemistry, Carl-von-Linne-Weg 10, D-5000 Koln 30, Federal Republic of Germany.

A small family of necrosis-inducing peptides has been identified as virulence factors of Rhynchosporium secalis, a fungal pathogen of barley (Hordeum vulgare L.) Two members of this family, NIP1 and NIP3, were found to stimulate the phosphohydrolyzing activity of the Mg2+-dependent, K+-stimulated H+-ATPase of plasma membrane vesicles isolated from barley leaves by partitioning in an aqueous two-phase system. Stimulation of enzyme activity was saturated by 10 to 15 [mu]M fungal protein. Another member of the peptide family, NIP2, did not affect the enzyme, indicating that it has a different mode of action.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12231685&dopt=Abstract [PubMed - as supplied by publisher]

Plant Physiol. 1993 Mar;101(3):819-824.
Alfalfa (Medicago sativa L.) Root Exudates Contain Isoflavonoids in the Presence of Rhizobium meliloti.

Dakora FD, Joseph CM, Phillips DA.

Department of Agronomy and Range Science, University of California, Davis, California 95616.

Root exudates of alfalfa (Medicago sativa L.) inoculated with symbiotic Rhizobium meliloti bacteria contained three isoflavonoids that were not found in exudates of uninoculated plants. Data from proton nuclear magnetic resonance, mass spectrometry, and ultraviolet-visible absorbance analyses indicated that root exudates of inoculated plants contained aglycone and glycoside forms of the phytoalexin medicarpin and a formononetin-7-O-(6"-O-malonylglycoside), a conjugated form of the medicarpin precursor formononetin. The medicarpin molecules did not induce nod gene transcription in R. meliloti, but the formononetin-7-O-(6"-O-malonylglycoside) induced nod genes regulated by both NodD1 and NodD2 proteins in R. meliloti. Hydrolysis of either the malonyl or the glycosyl linkage from the formononetin conjugate eliminated nod gene-inducing activity. The nod gene-inducing activity of crude root exudates was increased 200 and 65% upon inoculation with R. meliloti or R. leguminosarum bv phaseoli, respectively. When root exudate from uninoculated alfalfa was incubated with R. meliloti, high performance liquid chromatography analyses showed no evidence that bacterial metabolism produced medicarpin. These results indicate that alfalfa responds to symbiotic R. meliloti by exuding a phytoalexin normally elicited by pathogens and that the microsymbiont can use a precursor of the phytoalexin as a signal for inducing symbiotic nod genes.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12231731&dopt=Abstract [PubMed - as supplied by publisher]

Plant Physiol. 1993 Mar;101(3):873-880.
Sunflower (Helianthus annuus L.) Pathogenesis-Related Proteins (Induction by Aspirin (Acetylsalicylic Acid) and Characterization).

Jung JL, Fritig B, Hahne G.

Institut de Biologie Moleculaire des Plantes du Centre National de la Recherche Scientifique et Universite Louis Pasteur, 12 rue du General Zimmer, 67084 Strasbourg, France.

Sunflower leaf discs floated on a solution containing aspirin (acetylsalicylic acid) produced a set of new proteins extractable at pH 5.2 and excreted into the intercellular space. More than 80% of the proteins found in the intercellular fluids of induced leaf discs have been identified as pathogenesis-related (PR) proteins by their immunological relationship with tobacco PR proteins. Members of the four major classes of PR proteins have been characterized. Sunflower PR proteins of type 1 (PR1) and of type 3 (PR3) were found to have acidic isoelectric points, whereas the induced PR protein of type 2 (PR2) had a basic isoelectric point. Members of the type 5 PR proteins (PR5), known in tobacco as thaumatin-like proteins, showed a more complex pattern. Multiple sunflower PR5 isomers of similar molecular weight but of different isoelectric points were excreted from the cells in response to the aspirin treatment. PR2 and PR3 proteins were found at very low basal levels in untreated leaves, whereas PR1 and PR5 proteins could not be detected at all in the same extracts. Glucanase and chitinase activities were always associated with PR2 and PR3 proteins in partially purified sunflower extracts. All of these data indicate that, in response to aspirin treatment, sunflower plants produce a complete set of PR proteins characterized by an apparently exclusively extracellular localization.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12231738&dopt=Abstract [PubMed - as supplied by publisher]

Plant Physiol. 1993 Apr;101(4):1375-1380.
Induction of UDP-Glucose:Salicylic Acid Glucosyltransferase Activity in Tobacco Mosaic Virus-Inoculated Tobacco (Nicotiana tabacum) Leaves.

Enyedi AJ, Raskin I.

Center for Agricultural Molecular Biology, Cook College, Rutgers University, New Brunswick, New Jersey 08903-0231.

Salicylic acid (SA) is a putative signal that activates plant resistance to pathogens. SA levels increase systemically following the hypersensitive response produced by tobacco mosaic virus (TMV) inoculation of tobacco (Nicotiana tabacum L. cv Xanthi-nc) leaves. The SA increase in the inoculated leaf coincided with the appearance of a [beta]-glucosidase-hydrolyzable SA conjugate identified as [beta]-O-D-glucosylsalicylic acid (GSA). SA and GSA accumulation in the TMV-inoculated leaf paralleled the increase in the activity of a UDP-glucose:salicylic acid 3-O-glucosyltransferase (EC 2.4.1.35) ([beta]-GTase) capable of converting SA to GSA. Healthy tissues had constitutive [beta]-GTase activity of 0.076 milliunits g-1 fresh weight. This activity started to increase 48 h after TMV inoculation, reaching its maximum (6.7-fold induction over the basal levels) 72 h after TMV inoculation. No significant GSA or elevated [beta]-Gtase activity could be detected in the healthy leaf immediately above the TMV-inoculated leaf. The effect of TMV inoculation on the [beta]-GTase and GSA accumulation could be duplicated by infiltrating tobacco leaf discs with SA at the levels naturally produced in TMV-inoculated leaves (2.7-27.0 [mu]g g-1 fresh weight). Pretreatment of leaf discs with the protein synthesis inhibitor cycloheximide inhibited the induction of [beta]-GTase by SA and prevented the formation of GSA. Of 12 analogs of SA tested, only 2,6-dihydroxybenzoic acid induced [beta]-GTase activity.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12231791&dopt=Abstract [PubMed - as supplied by publisher]

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