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231224s2014 xx |||||o 00| ||eng c |
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|a 10.1016/j.plaphy.2013.10.031
|2 doi
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|a pubmed24n0776.xml
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|a (DE-627)NLM232940509
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|a (NLM)24262994
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|a (PII)S0981-9428(13)00381-1
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|a DE-627
|b ger
|c DE-627
|e rakwb
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| 041 |
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|a eng
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| 100 |
1 |
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|a Mazzeo, Maria Fiorella
|e verfasserin
|4 aut
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| 245 |
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|a Proteomic investigation of response to FORL infection in tomato roots
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|c 2014
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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| 338 |
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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| 500 |
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|a Date Completed 22.09.2014
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|a Date Revised 07.12.2022
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Copyright © 2013 Elsevier Masson SAS. All rights reserved.
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|a Fusarium oxysporum f. sp. radicis-lycopersici (FORL) leading to fusarium crown and root rot is considered one of the most destructive tomato soilborne diseases occurring in greenhouse and field crops. In this study, response to FORL infection in tomato roots was investigated by differential proteomics in susceptible (Monalbo) and resistant (Momor) isogenic tomato lines, thus leading to identify 33 proteins whose amount changed depending on the pathogen infection, and/or on the two genotypes. FORL infection induced accumulation of pathogen-related proteins (PR proteins) displaying glucanase and endochitinases activity or involved in redox processes in the Monalbo genotype. Interestingly, the level of the above mentioned PR proteins was not influenced by FORL infection in the resistant tomato line, while other proteins involved in general response mechanisms to biotic and/or abiotic stresses showed significant quantitative differences. In particular, the increased level of proteins participating to arginine metabolism and glutathione S-transferase (GST; EC 2.5.1.18) as well as that of protein LOC544002 and phosphoprotein ECPP44-like, suggested their key role in pathogen defence
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a 2-DE
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|a 2-DE maps
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|a FORL
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|a FORL infection
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|a Fusarium oxysporum f. sp. radicis-lycopersici
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|a GST
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|a IEF
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|a MALDI-TOF-MS
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|a MS/MS
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|a PR proteins
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|a Proteomics
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|a SDS-PAGE
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|a Tomato
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|a collision induced dissociation experiments
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|a electrospray ionization tandem mass spectrometry coupled with nano-reverse phase liquid chromatography
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|a glutathione S-transferase (EC 2.5.1.18)
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| 650 |
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4 |
|a isoelectric focusing
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4 |
|a m/z
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|a mass/charge
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|a matrix assisted laser desorption ionization-time of flight-mass spectrometry
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|a nano-HPLC-ESI-MS/MS
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|a pathogenesis-related proteins
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|a sodium dodecyl sulfate-polyacrylamide gel electrophoresis
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|a two-dimensional electrophoresis
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|a two-dimensional electrophoretic maps
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|a Plant Proteins
|2 NLM
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| 700 |
1 |
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|a Cacace, Giuseppina
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Ferriello, Francesca
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Puopolo, Gerardo
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Zoina, Astolfo
|e verfasserin
|4 aut
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| 700 |
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|a Ercolano, Maria Raffaella
|e verfasserin
|4 aut
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| 700 |
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|a Siciliano, Rosa Anna
|e verfasserin
|4 aut
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| 773 |
0 |
8 |
|i Enthalten in
|t Plant physiology and biochemistry : PPB
|d 1991
|g 74(2014) vom: 15. Jan., Seite 42-9
|w (DE-627)NLM098178261
|x 1873-2690
|7 nnns
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| 773 |
1 |
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|g volume:74
|g year:2014
|g day:15
|g month:01
|g pages:42-9
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|u http://dx.doi.org/10.1016/j.plaphy.2013.10.031
|3 Volltext
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|d 74
|j 2014
|b 15
|c 01
|h 42-9
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