Seed Storage Proteins of Faba Bean (Vicia faba L): Current Status and Prospects for Genetic Improvement

Abstract Background Recently quinoa( Chenopodium quinoa willd., 2n=4x=36)raises worldwide popularity with its totally nutrition, stress-tolerance, which leads quinoa to a strategic global food from an Andean native crop. However, seed pre-harvest sprouting, saponin contents e.c., restrict greatly quinoa production and popularity. In the study, we successfully used a combinational proteomics of TMT labeling and parallel reaction monitoring (PRM) to assess proteome changes relating to seed maturation conversion in quinoa to help accelerate genetic improvement for quinoa. Results In total, 6,097 proteins were identified and 4,770 proteins were quantified. Of them, 581 were differential expressed proteins (DEPs). Based on PRM data, seventeen DEPs were identified and quantified, including thirteen down-regulated proteins and four up-regulated proteins. Seventeen DEPs involved in oleanane-type saponins bio-synthesis (β-amyrin 28-oxidase), seed generation (β-Amylase), seed dormancy (late embryogenesis abundant proteins, Cyprosin), seed nutrition (globulin seed storage proteins), accumulation of sugars under seed desiccation (EARLY-RESPONSIVE TO DEHYDRATION 7 protein), pre-harvest sprouting (seed biotin-containing protein SBP65, ABA-inducible protein PHV A1), and enzymes related promoting seed maturation (bifunctional purple acid phosphatase 26), and pigment biosynthesis (3-O-glucosyltransferase). Conclusions We present the high-quality proteomics analysis of quinoa assessing proteome changes during seed maturation conversion. Our results summarize a valuable proteome profiles characterizing quinoa seed maturation. The DEPs are candidate for the functional analyses of proteins regulating seed maturation conversion in quinoa, which provide an important first step towards the genetic improvement of quinoa.

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Molecular heterogeneity and genetics of Vicia faba seed storage proteins

Theoretical and Applied Genetics ◽

10.1007/bf00226111 ◽

1991 ◽

Vol 81 (1) ◽

pp. 50-58 ◽

Cited By ~ 18

Author(s):

M. Tucci ◽

R. Capparelli ◽

A. Costa ◽

R. Rao

Keyword(s):

Vicia Faba ◽

Storage Proteins ◽

Seed Storage ◽

Seed Storage Proteins ◽

Molecular Heterogeneity

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Electrophoretic and immunochemical techniques for the molecular reassessment of relationships within Vicieae

Acta Agronomica Hungarica ◽

10.1556/aagr.55.2007.2.1 ◽

2007 ◽

Vol 55 (2) ◽

pp. 131-147

Author(s):

R. Sammour

Keyword(s):

Pisum Sativum ◽

Vicia Faba ◽

Cicer Arietinum ◽

Storage Proteins ◽

Seed Storage ◽

Seed Storage Proteins ◽

Immunochemical Study ◽

Partial Identity ◽

Electrophoretic Patterns ◽

Immunochemical Techniques

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 .

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