Proteomic analysis of rice defense response induced by probenazole

Institute of Plant and Microbial Biology, Academia Sinica, 128, Sec. 2, Academia Road, Taipei 11529, Taiwan.
Phytochemistry (Impact Factor: 3.35). 03/2008; 69(3):715-28. DOI: 10.1016/j.phytochem.2007.09.005
Source: PubMed

ABSTRACT Here, we report the first proteomic analysis of rice defense response induced by probenazole (PBZ), an agricultural chemical that has been widely used to protect rice plants from rice blast and the bacterial blight pathogen. Two-dimensional gel electrophoresis (2-DE) was utilized to identify a total of 40 protein spots including 9 protein spots that are up-regulated by PBZ and 31 abundant protein spots. A total of 11 unique proteins from these 9 spots were identified by LC-MS/MS, and the majority of them were classified and/or possessed orthologs in defense-related functions. Five protein spots with only one protein species identified in each spot appear to be PBZ-regulated proteins. They are a putative glutathione S-transferase GSTU17, a putative phenylalanine ammonia-lyase (PAL, XP_466843), a putative caffeic acid 3-O-methyltransferase (COMT), a putative NADH-ubiquinone oxidoreductase, and a putative glucose-1-phosphate adenyltransferase. However, the other six protein species identified from the remaining four protein spots could not be conclusively described as PBZ-regulated proteins due to either the co-migration of two protein species in one spot or the presence of one protein species in two spots. Through real-time reverse transcription polymerase chain reaction (RT-PCR), it was determined that PAL (XP_466843) is likely regulated at the protein level, whereas GSTU17 and COMT were regulated at the mRNA level after PBZ application. Interestingly, the mRNA transcripts of two PAL paralogs were found to be up-regulated by PBZ. We propose that PAL, COMT, and GSTU17 are likely to confer PBZ-induced disease resistance via such functions as biosynthesis and transport of flavonoid-type phytoalexin and/or lignin biogenesis.

  • Source
    • "The resulting peptides were desalted by use of ZIP-TIP (Millipore) and underwent liquid chromatography nano-electrospray ionization–tandem mass spectrometry (MS/MS) analysis (Q-TOF Ultima API MS; Micromass). The mass-to-charge ratios of precursor ions and MS/MS fragmented ions were processed as described (Lin et al., 2008). We identified proteins 4006 The Plant Cell using the Web-based search engine Mascot (http://www.matrixscience. "
    [Show abstract] [Hide abstract]
    ABSTRACT: Transcriptomic adjustment plays an important role in Arabidopsis thaliana seed germination and deetiolation in response to environmental light signals. The G-box cis-element is commonly present in promoters of genes that respond positively or negatively to the light signal. In pursuing additional transcriptional regulators that modulate light-mediated transcriptome changes, we identified bZIP16, a basic region/Leu zipper motif transcription factor, by G-box DNA affinity chromatography. We confirmed that bZIP16 has G-box-specific binding activity. Analysis of bzip16 mutants revealed that bZIP16 is a negative regulator in light-mediated inhibition of cell elongation but a positive regulator in light-regulated seed germination. Transcriptome analysis supported that bZIP16 is primarily a transcriptional repressor regulating light-, gibberellic acid (GA)-, and abscisic acid (ABA)-responsive genes. Chromatin immunoprecipitation analysis revealed that bZIP16 could directly target ABA-responsive genes and RGA-LIKE2, a DELLA gene in the GA signaling pathway. bZIP16 could also indirectly repress the expression of PHYTOCHROME INTERACTING FACTOR3-LIKE5, which encodes a basic helix-loop-helix protein coordinating hormone responses during seed germination. By repressing the expression of these genes, bZIP16 functions to promote seed germination and hypocotyl elongation during the early stages of Arabidopsis seedling development.
    The Plant Cell 10/2012; 24(10). DOI:10.1105/tpc.112.105478 · 9.58 Impact Factor
  • Source
    • "The pathogen-related (PR) proteins, especially the PR10 family, were found to be highly response to biotic stresses in several plants. One of the PR10 family proteins is the PBZ1, which was differentially regulated in response to probenazole, fungal elicitor, M. oryzae, X. oryzae, S. meliloti, and RYMV (Lin et al. 2008; Kim et al. 2003, 2004; Mahmood et al. 2006; Chi et al. 2010; Ventelon- Debout et al. 2004). Meanwhile, another PR10 family protein OsPR10 was also highly activated in response to multiple biotic stresses, including elicitor chitosan, CSB I, and fungal infection in SCCs and leaves (Agrawal et al. 2002; Liao et al. 2009; Kim et al. 2003, 2004). "
    [Show abstract] [Hide abstract]
    ABSTRACT: Biotic stresses affect the plant growth, seed quality, and crop yield. The monocot model rice crop plant is no exception and is affected by a variety of biotic stress factors. High-throughput proteomics approaches are being applied in rice for the past several years to exploit better understanding the biotic stresses-responsive regulatory mechanisms. A large number of proteins responsive to biotic stresses, including pathogens and herbivores, have been cataloged. Cataloged proteins mainly belong to functional categories into metabolism, energy, defense mechanisms, and signaling. To date, majority of these proteins have not been functionally characterized yet, except the pathogen-related 10 protein, PBZ1. This review will briefly summarize and discuss: (1) the proteomics-based investigation of biotic stress-responsive proteins in rice and (2) increasing importance of proteomics approach in defense biology and engineering the next-generation rice/crop plants. KeywordsBiotic stress–Rice–Proteomics
    Journal of Plant Biology 08/2011; 54(4):219-226. DOI:10.1007/s12374-011-9165-8 · 1.28 Impact Factor
  • Source
    • "The expression of another a-Hsp gene, shsp18, encoding a surface-exposed antigen of M. leprae (Ilangumaran et al., 1994; Lini et al., 2008), was activated in macrophages (Dellagostin et al., 1995). Our findings that the phytopathogen A. tumefaciens exploits the VirB-induced HspL expression to promote its tumorigenesis add to the list of a-Hsp participation in bacterial virulence. "
    [Show abstract] [Hide abstract]
    ABSTRACT: Agrobacterium tumefaciens is a Gram-negative plant-pathogenic bacterium that causes crown gall disease by transferring and integrating its transferred DNA (T-DNA) into the host genome. We characterized the chromosomally encoded alpha-crystallin-type small heat-shock protein (alpha-Hsp) HspL, which was induced by the virulence (vir) gene inducer acetosyringone (AS). The transcription of hspL but not three other alpha-Hsp genes (hspC, hspAT1, hspAT2) was upregulated by AS. Further expression analysis in various vir mutants suggested that AS-induced hspL transcription is not directly activated by the VirG response regulator but rather depends on the expression of VirG-activated virB genes encoding components of the type IV secretion system (T4SS). Among the 11 virB genes encoded by the virB operon, HspL protein levels were reduced in strains with deletions of virB6, virB8 or virB11. VirB protein accumulation but not virB transcription levels were reduced in an hspL deletion mutant early after AS induction, implying that HspL may affect the stability of individual VirB proteins or of the T4S complex directly or indirectly. Tumorigenesis efficiency and the VirB/D4-mediated conjugal transfer of an IncQ plasmid RSF1010 derivative between A. tumefaciens strains were reduced in the absence of HspL. In conclusion, increased HspL abundance is triggered in response to certain VirB protein(s) and plays a role in optimal VirB protein accumulation, VirB/D4-mediated DNA transfer and tumorigenesis.
    Microbiology 07/2009; 155(Pt 10):3270-80. DOI:10.1099/mic.0.030676-0 · 2.84 Impact Factor
Show more