Structural homology among the major 7s globulin subunits of soybean seed storage proteins

1986 ◽  
Vol 26 (1) ◽  
pp. 41-45 ◽  
Author(s):  
H. Hirano ◽  
H. Kagawa ◽  
Y. Kamata ◽  
F. Yamauchi
2004 ◽  
Vol 40 (2) ◽  
pp. 238-249 ◽  
Author(s):  
Takashi Mori ◽  
Nobuyuki Maruyama ◽  
Keito Nishizawa ◽  
Takahiko Higasa ◽  
Kazuhiro Yagasaki ◽  
...  

2003 ◽  
Vol 64 (3) ◽  
pp. 701-708 ◽  
Author(s):  
Nobuyuki Maruyama ◽  
Takako Fukuda ◽  
Shiori Saka ◽  
Nauko Inui ◽  
Junko Kotoh ◽  
...  

Plants ◽  
2021 ◽  
Vol 10 (4) ◽  
pp. 687
Author(s):  
Chan Seop Ko ◽  
Jin-Baek Kim ◽  
Min Jeong Hong ◽  
Yong Weon Seo

High-temperature stress during the grain filling stage has a deleterious effect on grain yield and end-use quality. Plants undergo various transcriptional events of protein complexity as defensive responses to various stressors. The “Keumgang” wheat cultivar was subjected to high-temperature stress for 6 and 10 days beginning 9 days after anthesis, then two-dimensional gel electrophoresis (2DE) and peptide analyses were performed. Spots showing decreased contents in stressed plants were shown to have strong similarities with a high-molecular glutenin gene, TraesCS1D02G317301 (TaHMW1D). QRT-PCR results confirmed that TaHMW1D was expressed in its full form and in the form of four different transcript variants. These events always occurred between repetitive regions at specific deletion sites (5′-CAA (Glutamine) GG/TG (Glycine) or (Valine)-3′, 5′-GGG (Glycine) CAA (Glutamine) -3′) in an exonic region. Heat stress led to a significant increase in the expression of the transcript variants. This was most evident in the distal parts of the spike. Considering the importance of high-molecular weight glutenin subunits of seed storage proteins, stressed plants might choose shorter polypeptides while retaining glutenin function, thus maintaining the expression of glutenin motifs and conserved sites.


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