The Effects of Wounding and Mite Infestation on Soybean Leaf Lipoxygenase Levels

1989 ◽  
Vol 44 (7-8) ◽  
pp. 655-659 ◽  
Author(s):  
David F. Hildebrand ◽  
Juan G. Rodriguez ◽  
Cindy S. Legg ◽  
Grayson C. Brown ◽  
Gerhard Bookjans

Numerous studies have demonstrated induction of proteins in plant tissues by wounding and infestations by various pests and pathogens. Lipoxygenase (LOX) is among the proteins that has been found to be induced by pathogens, but detailed information on the induction of LOX has not been reported. We have found a large (up to 10-fold) increase in LOX activity upon wounding of soybean (Glycine max L. Merr.) leaves and variable increases due to feeding of the twospotted spider mite. This induction in LOX activity was reflected in increases in amounts of both LOX protein and transcripts suggesting that the induction was at the transcriptional level. LOX activity was also found to be increased in unwounded leaves from plants with wounded leaves lower on the stem indicating that translocatable factors can cause remote induction of LOX activity.

1999 ◽  
Vol 34 (1) ◽  
pp. 132-143 ◽  
Author(s):  
T. C. Elden

Thirty-one soybean, Glycine max (L.) Merrill, accessions from maturity groups II through VIII were evaluated in excised and intact (whole plant) leaf bioassays to determine the ability of these bioassays to detect differences in susceptibility to the twospotted spider mite, Tetranychus urticae Koch. Although there were few significant differences between bioassays for variables measured within maturity groupings, the excised leaf bioassay which was easier to set up and monitor and took three-fourths less growth chamber space also had less variation among replications and repeated tests and detected a greater number of differences among accessions. Although there were significant differences among soybean accessions within a maturity group for specific variables, results suggest that high levels of resistance to the twospotted spider mite are not present in the germplasm screened. Several accessions screened, with known resistance to foliar feeding insects, were significantly less preferred for spider mite oviposition and development. However, it was apparent that the gene(s) controlling insect resistance do not impart the same level of resistance to the twospotted spider mite. Results of this study, based on differences in susceptibility among soybean accessions, demonstrate that the excised leaf bioassay should prove to be an efficient and uniform laboratory bioassay to screen soybean germplasm for resistance to the twospotted spider mite.


2021 ◽  
Vol 22 (2) ◽  
pp. 920
Author(s):  
Ling Cheng ◽  
Wanling Min ◽  
Man Li ◽  
Lili Zhou ◽  
Chuan-Chih Hsu ◽  
...  

Soybean (Glycine max L.) is a major crop providing important source for protein and oil for human life. Low phosphate (LP) availability is a critical limiting factor affecting soybean production. Soybean plants develop a series of strategies to adapt to phosphate (Pi) limitation condition. However, the underlying molecular mechanisms responsible for LP stress response remain largely unknown. Here, we performed a label-free quantification (LFQ) analysis of soybean leaves grown under low and high phosphate conditions. We identified 267 induced and 440 reduced differential proteins from phosphate-starved leaves. Almost a quarter of the LP decreased proteins are involved in translation processes, while the LP increased proteins are accumulated in chlorophyll biosynthetic and carbon metabolic processes. Among these induced proteins, an enolase protein, GmENO2a was found to be mostly induced protein. On the transcriptional level, GmENO2a and GmENO2b, but not GmENO2c or GmENO2d, were dramatically induced by phosphate starvation. Among 14 enolase genes, only GmENO2a and GmENO2b genes contain the P1BS motif in their promoter regions. Furthermore, GmENO2b was specifically induced in the GmPHR31 overexpressing soybean plants. Our findings provide molecular insights into how soybean plants tune basic carbon metabolic pathway to adapt to Pi deprivation through the ENO2 enzymes.


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