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. 2018 Jan 12;10(1):41.
doi: 10.3390/toxins10010041.

Transketolase Is Identified as a Target of Herbicidal Substance α-Terthienyl by Proteomics

Bin Zhao  1   2 , Jingqian Huo  3 , Ning Liu  4 , Jinlin Zhang  5 , Jingao Dong  6
Affiliations

Transketolase Is Identified as a Target of Herbicidal Substance α-Terthienyl by Proteomics

Bin Zhao et al. Toxins (Basel). .

Abstract

α-terthienyl is a natural phytotoxin isolated originally from Flaveria bidentis (L.) Kuntze. The bioassay presented here shows the strong herbicidal activity of α-terthienyl on Digitaria sanguinalis, Arabidopsis thaliana and Chlamydomonas reinhardtii. The α-terthienyl-induced response of A. thaliana at the protein level was analyzed at different times. Changes in the protein expression profiles were analyzed by two-dimensional gel electrophoresis and liquid chromatography tandem mass spectrometry (LC-MS/MS) mass spectrometry. Sixteen protein spots were identified that showed reproducible changes in the expression of at least 2-fold when compared to the control. Among these 16 spots, three were up-regulated and 13 were down-regulated. The decreased expression of several proteins associated with energy production and carbon metabolism suggested that these processes were affected by α-terthienyl. To search for the candidate proteins in this screen, A. thaliana T-DNA mutants of the candidate proteins were used to test their susceptibility to α-terthienyl. Amongst the others, attkl1, a mutant of transketolase, exhibited a significantly lower sensitivity to α-terthienyl when hit compared with Col-0. Based on the identification of the proteins associated with the response to α-terthienyl by proteomics, a candidate target protein transketolase was identified.

Keywords: herbicidal mechanism; proteomics; transketolase; α-terthienyl.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
Structural formula of α-terthienyl.
Figure 2
Figure 2
Distribution of expressed proteins (DEPs) in PAGE gel. (A) Treated by α-terthienyl for 0 h; (B) treated by α-terthienyl for 0.5 h; (C) treated by α-terthienyl for 2 h; (D) treated by α-terthienyl for 6 h.
Figure 3
Figure 3
DEPs regulated by α-terthienyl.
Figure 4
Figure 4
Protein-protein interaction regulatory network of DEPs. The regulatory network of DEPs was done using String software. Differentially regulatory network was represented by node. Different colors of lines represent different evidences for the predicted functional relationship between proteins; red line, gene fusions; dark blue line, gene co-occurrence; black line, co-expression; yellow line, text mining; green line, gene neighborhood; light blue line, database; and pink line, experimentally determined.
Figure 5
Figure 5
The identification of different expression proteins by Quantitative Real-Time PCR (Q-PCR).
Figure 6
Figure 6
The sensitivity of Arabidopsis mutant to α-terthienyl.
Figure 7
Figure 7
The enzyme activity of Col-0 and attkl1 which was treated by α-terthienyl.
See this image and copyright information in PMC

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