Molecular heterogeneity and genetics of Vicia faba seed storage proteins

1991 ◽  
Vol 81 (1) ◽  
pp. 50-58 ◽  
Author(s):  
M. Tucci ◽  
R. Capparelli ◽  
A. Costa ◽  
R. Rao
1994 ◽  
Vol 191 (1-2) ◽  
pp. 39-56 ◽  
Author(s):  
Martin Fotso ◽  
Jean-Louis Azanza ◽  
Remy Pasquet ◽  
Jacques Raymond

3 Biotech ◽  
2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Yujiao Liu ◽  
Xuexia Wu ◽  
Wanwei Hou ◽  
Ping Li ◽  
Weichao Sha ◽  
...  

2007 ◽  
Vol 55 (2) ◽  
pp. 131-147
Author(s):  
R. Sammour

In this study, an array of electrophoretic and immunochemical techniques was used to investigate the legumins, vicilins and albumins of seed storage proteins in Pisum sativum , Vicia faba , Lens esculentum , and Cicer arietinum to delimit the boundary of the tribe Vicieae and to clarify the systematic position of the genus Cicer . The band patterns of the legumins of these species were broadly similar in that they had bands at Mr 60 kDa which disappeared in the presence of 2-mercaptoethanol, giving rise to two sets of new bands, at Mr approximately 40 kDa and 20 kDa, representing acidic or α and basic or β subunits. The band patterns of the vicilins were also quite similar in that they showed bands at Mr approximately 71 kDa (convicilin) and 50 kDa (vicilin), which were not altered by the presence of 2-mercaptoethanol. Serologically, the legumins of Vicia faba and Lens esculentum exhibited total identity with Pisum legumin antiserum under nonreducing conditions, whereas the legumin of Cicer arietinum exhibited only partial identity, which was attributed to the failure of the low molecular subunit pair (Mr 33 kDa) to react with Pisum legumin antiserum. On the other hand, the vicilins of Vicia faba , Lens esculentum and Cicer arietinum had only partial identity with the vicilin of Pisum sativum , which was due to the failure of a number of subunits along the electrophoretic patterns of these species to react with Pisum sativum vicilin antiserum. The electrophoretic patterns of Vicia faba , Lens esculentum and Cicer arietinum were markedly different for the albumins. However, immunochemically they gave a positive reaction with Pisum major albumin antiserum (Mr 25 kDa) and showed a band with a molecular weight slightly higher than the major albumin of Pisum sativum . Extending the immunochemical study to members of the Phaseoleae, Glycineae, Cajaneae and Diocleae revealed that the vicilin and legumin of Cicer were more closely related to the Vicieae than to these tribes. Thus the data presented in this work recommended the classification of Cicer under Vicieae rather than as a separate tribe Cicerideae .


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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