| Literature DB >> 20705057 |
Chan Ju Lim1, Woong Bom Kim, Bok-Sim Lee, Ha Youn Lee, Tae-Ho Kwon, Jeong Mee Park, Suk-Yoon Kwon.
Abstract
As a heterodimeric protein, ferredoxin:thioredoxin reductase (FTR) catalyses the light-dependant activation of several photosynthetic enzymes. The active site of the catalytic subunit of FTR contains a redox-active disulfide and a [4Fe-4S] center. We isolated the catalytic subunit gene of FTR, designated SlFTR-c, from tomato (Solanum lycopersicum L.). SlFTR-c transcripts were detected in all tissues examined, including roots, leaves, flowers, fruits, and seeds. Interestingly, virus-induced gene silencing (VIGS) of SlFTR-c resulted in necrotic lesions with typical cell death symptoms and reactive oxygen species (ROS) production in tomato leaves. Moreover, these SlFTR-c-silenced plants displayed enhanced disease resistance against bacterial pathogens, specifically Pseudomonas syringae pv. tomato DC3000, by the induction of defense-related genes (SlPR-1, SlPR-2, SlPR-5, SlGlucA, SlChi3, and SlChi9). Taken together, it seems that SlFTR-c works as a regulator of programmed cell death (PCD) and pathogen resistance in tomato plants. Copyright 2010 Elsevier Inc. All rights reserved.Entities:
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Year: 2010 PMID: 20705057 DOI: 10.1016/j.bbrc.2010.08.016
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575