Molecular and structural analysis of electrophoretic variants of soybean seed storage proteins

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

2016 ◽  
Vol 2016 ◽  
pp. 1-11 ◽  
Author(s):  
Jose C. Jimenez-Lopez ◽  
Adoración Zafra ◽  
Lucía Palanco ◽  
José Fernando Florido ◽  
Juan de Dios Alché

Olive seeds, which are a raw material of interest, have been reported to contain 11S seed storage proteins (SSPs). However, the presence of SSPs such as 7S vicilins has not been studied. In this study, following a search in the olive seed transcriptome, 58 sequences corresponding to 7S vicilins were retrieved. A partial sequence was amplified by PCR from olive seed cDNA and subjected to phylogenetic analysis with other sequences. Structural analysis showed that olive 7S vicilin contains 9α-helixes and 22β-sheets. Additionally, 3D structural analysis displayed good superimposition with vicilin models generated fromPistaciaandSesamum. In order to assess potential allergenicity, T and B epitopes present in these proteins were identified by bioinformatic approaches. Different motifs were observed among the species, as well as some species-specific motifs. Finally, expression analysis of vicilins was carried out in protein extracts obtained from seeds of different species, including the olive. Noticeable bands were observed for all species in the 15–75 kDa MW interval, which were compatible with vicilins. The reactivity of the extracts to sera from patients allergic to nuts was also analysed. The findings with regard to the potential use of olive seed as food are discussed.


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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