Identification of differentially expressed proteins in wheat after benzothiadiazole treatment

2012-12-01
Gunel, Aslihan
Asbahi, Adnan
Ozgazi, Nese
Akkaya, Mahinur
The systemic acquired resistance (SAR) mechanism is stimulated by biological and chemical agents in response to pathogen infection as a part of the innate immunity response system of plants. The externally applied synthetic chemical, benzo-(1,2,3)-thiadiazole-7-carbothioic acid-S-methyl ester (BTH), is also known to induce a SAR response in plants. Studies identifying genes induced or suppressed by BTH are limited. Only few genes responding to BTH are determined. The focus of this preliminary study is to identify the gene products affected by BTH in wheat. A 2D-polyacrylamide gel electrophoresis (PAGE) analysis was carried out with BTH treated Triticum aestivum cv. Gerek-79 and mock treated samples. Following 2D-PAGE image analysis, the selected differentially expressed protein spots were identified by nanoLC-ESI-MS/MS. Among the 26 protein spots distinguished, five were found to be increased upon BTH treatment, another set of seven spots were absent in the control sample.Thus, they were apparent only in the gel of the BTH treated sample (+BTH), whereas five protein spots disappeared in the gel of the BTH treated plants (-BTH). Up-regulation of some proteins such as OEE2 (oxygen evolving enhancer protein) and COR (cold-responsive) LEA (late embryogenesis abundant)/RAB (responsive to abscisic acid, ABA) and down-regulation of some proteins such as RuBisCo LSU (large subunit), fructose 1, 6-biphosphate aldolase (AldP), methyl binding domain protein 6 (MBD6), and 3-isopropylmalate dehydrogenase are shown for the first time in BTH treatment of wheat.
JOURNAL OF PLANT DISEASES AND PROTECTION

Suggestions

Identification and characterization of hydrolytic enzymes from the midgut of Sunn Pest of wheat (Eurygaster integriceps)
Ogur, E.; YÜCEL, MUSTAFA; Öktem, Hüseyin Avni (Informa UK Limited, 2009-01-01)
To help in the development of Sunn Pest-resistant transgenic plants employing protease or alpha-amylase inhibitors, midgut hydrolytic enzymes of Sunn Pest (Eurygaster integriceps, Put.) (Heteroptera: Scutelleridae) were identified and characterized biochemically. We observed levels of very low proteolytic activity of trypsin (3 nmoles/min/mg), elastase (0.66 nmoles/min/mg) and leucine aminopeptidase-like (14.4 nmoles/min/mg) proteases, but no chymotrypsin and papain-like activity. Proteolytic activities wer...
Characterization of extracellular beta-lactamases from penicillin G-resistant cells of Streptococcus thermophilus
Chirica, LC; Güray, Nülüfer Tülün; Gültekin, Güzin Candan; Bozoglu, F (International Association for Food Protection, 1998-07-01)
In this study, biochemical properties of two extracellular beta-lactamases produced by penicillin-resistant Streptococcus thermophilus cells were investigated. Both beta-lactamases showed specificity for penicillins but not for cephaloridins. The p-lactamases exhibited different affinities for penicillin G. The one with the higher molecular weight (F1) had a K(m) value of 3.44 mu M and a V(max), value of 8.33, mu mol/min/mg of protein, whereas the beta-lactamase with the lower molecular weight (FII) had a K...
Isolation and immunological characterization of theta class glutathione-s-transferase gstt2-2 from bovine liver
İşgör, Sultan Belgin; Çoruh, Nursen; Department of Biochemistry (2004)
The glutathione-S-transferases (GSTs) (EC.2.5.1.18) are enzymes that participate in cellular detoxification of endogenous as well as foreign electrophilic compounds, function in the cellular detoxification systems and are evolved to protect cells against reactive oxygen metabolites by conjugating the reactive molecules to the nucleophile scavenging tripeptide glutathione (GSH, ?-glu-cys-gly). The GSTs are found in all eukaryotes and prokaryotic systems, in the cytoplasm, on the microsomes, and in the mitoch...
Discovery of non-carbohydrate inhibitors of aminoglycoside-modifying enzymes
Welch, KT; Virga, KG; Whittemore, NA; Özen, Can; Wright, E; Brown, CL; Lee, RE; Serpersu, EH (2005-11-15)
Chemical modification and inactivation of aminoglycosides by many different enzymes expressed in pathogenic bacteria are the main mechanisms of bacterial resistance to these antibiotics. In this work, we designed inhibitors that contain the 1,3-diamine pharmacophore shared by all aminoglycoside antibiotics that contain the 2-deoxystreptamine ring. A discovery library of molecules was prepared by attaching different side chains to both sides of the 1,3-diamine motif. Several of these diamines showed inhibito...
Identification of R Plasmids of Pseudomonas aeruginosa isolates from clinical sources by recombinant DNA techniques
İzgü, Kadri Fatih (1994-01-01)
The R-plasmids, which transfer resistance to p. aeruginosa strains agaiiıst generally used antibiotics in the treatmet of the infections caıısed by this gram (-) bacteria were investigated. The P. aeruginosa samples used in this study were isolat-ed from the clinical cases of Gülhane Military Medical Academy (GATA), such as throat, ear and urinary tract infections. Those clinical specimens of P. aeruginosa were tested far their sensitivities to fourteen different antibiotics that are used against P. aeurigo...
Citation Formats
A. Gunel, A. Asbahi, N. Ozgazi, and M. Akkaya, “Identification of differentially expressed proteins in wheat after benzothiadiazole treatment,” JOURNAL OF PLANT DISEASES AND PROTECTION, pp. 182–190, 2012, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/51787.