Comparison of Gene Families: Seed Storage and Other Seed Proteins

Joshi, Jaya; Pandurangan, Sudhakar; Diapari, Marwan; Marsolais, Frédéric

doi:10.1007/978-3-319-63526-2_10

Cited by 11 publications

(11 citation statements)

References 102 publications

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“…The concentration of S-AA is strongly related to the relative proportions of S-AA rich proteins in the seeds. In Vf and other legumes, it is well accepted that legumins contain relatively higher S-AA compared to vicilin 42,44,[57][58] . This is further confirmed by comparative analysis of coding sequences of vicilin and legumin subunits across legume species which clearly show that legumin subunits contain more residues of cysteine and methionine ( Figure 4).…”

Section: Structure and Composition Of Vf Globulinsmentioning

confidence: 99%

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

Warsame

O’Sullivan

Tosi

2018

J. Agric. Food Chem.

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Faba bean (Vicia faba, L.) is one of the foremost candidate crops for simultaneously increasing both sustainability and global supply of plant protein. Its seeds contain about 27% proteins of which more than 80%-consist of globulin storage proteins (vicilin and legumin). For optimum utilization for human and animal nutrition, both protein content and quality have to be improved. Though initial investigations on the hereditability of these traits indicated possibility for genetic improvement, little has been achieved so far partly due to lack of genetic information coupled with the complex relationship between protein content and grain yield. This review reports on the current knowledge on faba bean seed storage proteins; their structure, composition and genetic control and highlights key areas for further improvement of the content and composition of faba bean seed storage proteins on the basis of recent advances in faba bean genome knowledge and genetic tools.

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Section: Structure and Composition Of Vf Globulinsmentioning

confidence: 99%

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

Warsame

O’Sullivan

Tosi

2018

J. Agric. Food Chem.

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“…By way of illustration, approximately 70–80% of the total amount of reduced nitrogen in cereals and legume grains can be attributed to seed storage proteins (SSPs) [ 10 ]. In addition, some SSPs and vegetative storage proteins (VSPs) can exhibit additional enzymatic activities such as lipid acyl hydrolase, acyltranferase, esterase and acid phosphatase activities capable of assuming useful supplementary biological functions, including defense and antioxidant functions [ 11 , 12 , 13 , 14 ].…”

Section: Introductionmentioning

confidence: 99%

“…Seed proteome comprises a heterogeneous collection of functionally differentiated proteins that undergo highly dynamic qualitative and quantitative changes in order to meet seed requirements during development and germination. Storage proteins are typically multimeric proteins encoded by multi-gene families constituted by highly homologous genes clustered on one or various chromosomes [ 14 , 20 , 27 , 28 ]. They often undergo abundant glycosylations and phosphorylations, two types of co- and/or post-translational modifications (PTMs) that notably increase the diversity of isoforms [ 29 , 30 ].…”

Section: Introductionmentioning

confidence: 99%

Advances in the Biology of Seed and Vegetative Storage Proteins Based on Two-Dimensional Electrophoresis Coupled to Mass Spectrometry

et al. 2018

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Seed storage proteins play a fundamental role in plant reproduction and human nutrition. They accumulate during seed development as reserve material for germination and seedling growth and are a major source of dietary protein for human consumption. Storage proteins encompass multiple isoforms encoded by multi-gene families that undergo abundant glycosylations and phosphorylations. Two-dimensional electrophoresis (2-DE) is a proteomic tool especially suitable for the characterization of storage proteins because of their peculiar characteristics. In particular, storage proteins are soluble multimeric proteins highly represented in the seed proteome that contain polypeptides of molecular mass between 10 and 130 kDa. In addition, high-resolution profiles can be achieved by applying targeted 2-DE protocols. 2-DE coupled with mass spectrometry (MS) has traditionally been the methodology of choice in numerous studies on the biology of storage proteins in a wide diversity of plants. 2-DE-based reference maps have decisively contributed to the current state of our knowledge about storage proteins in multiple key aspects, including identification of isoforms and quantification of their relative abundance, identification of phosphorylated isoforms and assessment of their phosphorylation status, and dynamic changes of isoforms during seed development and germination both qualitatively and quantitatively. These advances have translated into relevant information about meaningful traits in seed breeding such as protein quality, longevity, gluten and allergen content, stress response and antifungal, antibacterial, and insect susceptibility. This review addresses progress on the biology of storage proteins and application areas in seed breeding using 2-DE-based maps.

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“…The 7S globulin, phaseolin, normally constitutes approximately half of total seed protein in cultivated varieties of common bean (Vitale & Bollini, 1995). Phaseolins are encoded by a single, complex locus on chromosome 7 containing multiple genes in tandem (Joshi et al, 2017; Pandurangan & Marsolais, 2017; Talbot et al, 1984). Despite the fact that phaseolins have few methionine residues, it was previously reported that the total concentration of methionine is positively correlated with phaseolin levels, since they are so abundant in seed (Gepts & Bliss, 1984).…”

Section: Introductionmentioning

confidence: 99%

Common bean (Phaseolus vulgaris L.) with increased cysteine and methionine concentration

et al. 2021

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In common bean (Phaseolus vulgaris L.), seed storage protein deficiency is associated with increased total cysteine and methionine concentration. The goal of this study was to generate germplasm lines that combine this characteristic with adaptation to short season conditions in Manitoba, Canada. A recombinant inbred line population was developed by crossing the storage protein deficient genotype, SMARC1N‐PN1 with the cultivar Morden003. Two lines, 2‐37 and 3‐84, with a stable protein profile over 2 years at two locations were identified. Like SMARC1N‐PN1, both lines had a significantly higher cysteine concentration than Morden003, by approximately 35%. Methionine levels were elevated by approximately 15%, while tryptophan levels were also increased by approximately 30%. Line 2‐37 had a significant increase in protein quality, as measured by in vitro protein digestibility corrected amino acid score, by approximately 40%, as compared with Morden003. The increased protein quality for this line is attributable to higher levels of total cysteine and methionine, while having an overall reduction in crude protein concentration. Line 2‐37 had a similar seed yield as SMARC1N‐PN1, with a maturity comparable to Morden003. The results of high‐density single nucleotide polymorphism (SNP) genotyping and quantitative trait locus analysis of recombinant inbred lines indicated that variation in cysteine concentration was determined by the phaseolin locus, while variation in methionine concentration was determined by both the phaseolin and lectin loci. SNP markers that track the introgression of phaseolin and lectin deficiency into the Morden003 background were identified and validated.

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Comparison of Gene Families: Seed Storage and Other Seed Proteins

Cited by 11 publications

References 102 publications

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

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

Advances in the Biology of Seed and Vegetative Storage Proteins Based on Two-Dimensional Electrophoresis Coupled to Mass Spectrometry

Common bean (Phaseolus vulgaris L.) with increased cysteine and methionine concentration

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