ABSTRACT
The nitric oxide (NO) donor sodium nitroprusside upregulated the proline iminopeptidase content in the pea seedling roots. It is assumed that NO activates deprolinization of the proline-rich proteins, as evidenced by an increase in the content of free proline, which is known to protect plants from the abiotic and biotic stressors.
Subject(s)
Nitric OxideABSTRACT
Three proteins induced by salicylic acid were revealed in pea roots. These proteins were identified as chitinase isozymes belonging to the glycoside hydrolases family 18. The PsCam050724 transcript encoding at least one of these isoforms was found, allowing us to determine its primary structure, which lacks the signal peptide.
Subject(s)
Chitinases/biosynthesis , Gene Expression Regulation, Enzymologic/drug effects , Pisum sativum/drug effects , Pisum sativum/enzymology , Salicylic Acid/pharmacology , Anti-Infective Agents/pharmacology , Chitinases/genetics , Chitinases/metabolism , Electrophoresis, Gel, Two-Dimensional/methods , Enzyme Induction/drug effects , Pisum sativum/genetics , Plant Roots/drug effects , Plant Roots/enzymology , Plant Roots/genetics , Proteomics/methodsABSTRACT
The treatment of pea roots with azelaic acid for 72 h led to a change in the content of 28 proteins: the content of 20 proteins decreased, and the content of 8 proteins (including the phenylpropanoid metabolism enzymes, which are involved in the synthesis of phytoalexins) increased.
Subject(s)
Defense Mechanisms , Dicarboxylic Acids/pharmacology , Phenols , Pisum sativum , Plant Roots/chemistry , Sesquiterpenes/metabolism , Phenols/metabolism , Plant Roots/drug effects , PhytoalexinsSubject(s)
Acetates/pharmacology , Cyclopentanes/pharmacology , Oxylipins/pharmacology , Pisum sativum/drug effects , Plant Growth Regulators/pharmacology , Plant Roots/drug effects , Proteomics , Seedlings/drug effects , Pisum sativum/metabolism , Plant Proteins/metabolism , Plant Roots/metabolism , Seedlings/metabolismABSTRACT
The effect of 50 microM salicylic acid on soluble proteins of pea (Pisum sativum L.) leaves was studied by proteomic analysis. Thirty-two salicylate-induced proteins were found, and 13 of these were identified using MALDI TOF MS. Salicylate-induced increased content was shown for the first time for the family 18 glycoside hydrolase, alpha-amylase, 33 kDa protein of photosystem II, lipid-desaturase-like protein, and glutamine amidotransferase. Increased content of protective proteins of direct antipathogenic action such as chitinase and beta-1,3-glucanases was also noted.
Subject(s)
Pisum sativum/metabolism , Plant Proteins/biosynthesis , Proteome/analysis , Salicylic Acid/pharmacology , Electrophoresis, Gel, Two-Dimensional , Pisum sativum/drug effects , Plant Leaves/drug effects , Plant Leaves/metabolism , Proteomics , Spectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationSubject(s)
Apoptosis/drug effects , Pisum sativum/physiology , Plant Proteins/metabolism , Plant Roots/physiology , Proteome/metabolism , Salicylates/administration & dosage , Dose-Response Relationship, Drug , Gene Expression Regulation, Plant/drug effects , Gene Expression Regulation, Plant/physiology , Pisum sativum/drug effects , Plant Roots/drug effectsSubject(s)
Pisum sativum/drug effects , Plant Proteins , Plant Roots/drug effects , Salicylates/pharmacology , Electrophoresis, Gel, Two-Dimensional , Pisum sativum/metabolism , Plant Proteins/chemistry , Plant Proteins/metabolism , Plant Roots/metabolism , Spectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationABSTRACT
Brassinosteroid-induced phosphorylation of tyrosine residues in proteins was studied. Proteins of crude extract of pea leaves were analyzed by one- and two-dimensional electrophoresis followed by Western blotting with monoclonal antibodies PY20 to phosphotyrosine proteins. One- and two-dimensional electrophoresis revealed 7 and 13 tyrosine-phosphorylated proteins, respectively. Brassinolide increased the phosphorylation level of most of these proteins. With inhibitors of tyrosine protein phosphatases, such as phenylarsine oxide and orthovanadate, the level of tyrosine phosphorylation of these proteins increased.
Subject(s)
Cholestanols/pharmacology , Pisum sativum/metabolism , Plant Growth Regulators/pharmacology , Plant Proteins/metabolism , Steroids, Heterocyclic/pharmacology , Tyrosine/metabolism , Brassinosteroids , Cholestanols/metabolism , Electrophoresis, Gel, Two-Dimensional , Molecular Weight , Pisum sativum/cytology , Phosphorylation , Plant Growth Regulators/metabolism , Plant Leaves/cytology , Plant Leaves/drug effects , Plant Leaves/metabolism , Steroids, Heterocyclic/metabolismSubject(s)
Lipoxygenase/metabolism , Plant Growth Regulators/pharmacology , Plant Proteins/metabolism , Signal Transduction , Steroids, Heterocyclic/pharmacology , Cholestadienols/pharmacology , Linoleic Acids/chemistry , Pisum sativum/chemistry , Phospholipases A/antagonists & inhibitors , Phosphorylation/drug effects , PhytosterolsABSTRACT
All investigated exogenous phytohormones (jasmonic, salicylic, and abscisic acids) induced the appearance of (14)C-label in a polypeptide with molecular mass 29 kD that was not found in the control; these acids also increased [(14)C]leucine incorporation into a 25-kD polypeptide and decreased such incorporation into a 45-kD polypeptide. This can be considered as a nonspecific response of the plants to the action of these hormones. Salicylic and abscisic (but not jasmonic) acids induced the synthesis of a 19-kD polypeptide, and jasmonate induced the synthesis of a 96-kD polypeptide.
Subject(s)
Abscisic Acid/pharmacology , Cyclopentanes/pharmacology , Leucine/metabolism , Plant Leaves/metabolism , Plant Proteins/metabolism , Salicylic Acid/pharmacology , Carbon Radioisotopes , Oxylipins , Pisum sativumABSTRACT
The products of the lipoxygenase pathway, methyl jasmonic acid (MeJA) and (9Z)-12-hydroxy-9-dodecenoic acid (HDA), hardly changed the relative level of phosphorylated polypeptides (RLPPs) during 2 h of incubation: 15 and 17 kDa RLPPs were enhanced by HDA, but decreased by MeJA. RLPPs of 73 and 82 kDa were increased by both compounds. MeJA and HDA treatment induced specific and unspecific effects in some RLPPs. It was shown that HDA and MeJA increased protein kinase activity in the presence of 1 microM cAMP.
Subject(s)
Acetates/pharmacology , Cyclopentanes/pharmacology , Fatty Acids, Monounsaturated/pharmacology , Phosphates/metabolism , Pisum sativum/metabolism , Plant Growth Regulators/pharmacology , Plant Proteins/metabolism , Oxylipins , Pisum sativum/drug effects , Phosphopeptides/metabolism , Phosphorylation , Plant Leaves/metabolismABSTRACT
Chitinase and proteinase activities were found in aphroproteins excreted by larvae of the cicada Aphrophora costalis Mats; this accounts for their fungicidal effect. Aphroproteins did not show DNase or RNase activities and did not exhibit properties of proteinase inhibitors. The data suggest that larval foam protects the larva and host plant from entomogenous and phytopathogenic fungi.
Subject(s)
Chitinases/metabolism , Endopeptidases/metabolism , Insect Proteins/metabolism , Serratia marcescens/enzymologyABSTRACT
The potato tuber lipoxygenase preparations convert alpha-linolenic acid not only to 9(S)-HPOTE, but also to some more polar metabolites. Two of these polar products, I and II, with ultraviolet absorbance maxima at 267 nm were purified by HPLC. It was found that metabolites I and II have, respectively, one and two hydroperoxy groups. Products of NaBH4 reduction of both I and II were identified by their chemical ionization and electron impact mass spectra and by 1H-NMR spectra as 9,16-dihydroxy-10(E), 12(Z), 14(E)-octadecatrienoic acid. The obtained results suggest that compound II is 9.16-dihydroperoxy-10(E), 12(Z), 14(E)-octadecatrienoic acid and product I is a mixture of two positional isomers, 9-hydroxy-16-hydroperoxy-10(E),12(Z),14(E)-octadecatrienoic and 9-hydroperoxy-16-hydroxy-10(E),12(Z),14(E)-octadecatrienoic acids. Lipoxygenase converts efficiently [14C]9-HOTE into product I. Also, both metabolites I and II are the products of double dioxygenation. The second oxygenation at C-16 position as well as the first one at C-9 is controlled by lipoxygenase.