Redox Changes Accompanying the Degradation of Seed Storage Proteins in Germinating Rice

Yano, Hiroyuki; Wong, Joshua; Cho, Myeong‐Je; Buchanan, Bob B.

doi:10.1093/pcp/pce119

Cited by 67 publications

(56 citation statements)

References 24 publications

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“…These proteins were also found to undergo reduction during germination. Similar results were obtained with barley (Marx et al, 2003) and other types of seeds, notably an albumin of castor and an albumin, a conglutin, and a glycinin of peanut (Shin et al, 1993;Yano et al, 2001a). It is thus not surprising that water-soluble storage proteins were found to be Trx targets in M. truncatula: 2S albumin, conglutin, and several legumins (Table II); albumin and legumins A and J being reduced during germination (Fig.…”

Section: Storage Proteinssupporting

confidence: 83%

“…Proteins of both the starchy endosperm and embryo that are present mainly in the oxidized (S-S) form in the dry seed are converted to the reduced or sulfhydryl (SH) state following imbibition Lozano et al, 1996;Gobin et al, 1997;Yano et al, 2001a;De Gara et al, 2003;Marx et al, 2003;Rhazi et al, 2003). The regulatory disulfide protein, thioredoxin (Trx), appears to play a central role in the redox conversion.…”

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Thioredoxin-Linked Proteins Are Reduced during Germination ofMedicago truncatulaSeeds

et al. 2007

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Germination of cereals is accompanied by extensive change in the redox state of seed proteins. Proteins present in oxidized form in dry seeds are converted to the reduced state following imbibition. Thioredoxin (Trx) appears to play a role in this transition in cereals. It is not known, however, whether Trx-linked redox changes are restricted to cereals or whether they take place more broadly in germinating seeds. To gain information on this point, we have investigated a model legume, Medicago truncatula. Two complementary gel-based proteomic approaches were followed to identify Trx targets in seeds: Proteins were (1) labeled with a thiol-specific probe, monobromobimane (mBBr), following in vitro reduction by an NADP/Trx system, or (2) isolated on a mutant Trx affinity column. Altogether, 111 Trx-linked proteins were identified with few differences between axes and cotyledons. Fifty nine were new, 34 found previously in cereal or peanut seeds, and 18 in other plants or photosynthetic organisms. In parallel, the redox state of proteins assessed in germinating seeds using mBBr revealed that a substantial number of proteins that are oxidized or partly reduced in dry seeds became more reduced upon germination. The patterns were similar for proteins reduced in vivo during germination or in vitro by Trx. In contrast, glutathione and glutaredoxin were less effective as reductants in vitro. Overall, more than half of the potential targets identified with the mBBr labeling procedure were reduced during germination. The results provide evidence that Trx functions in the germination of seeds of dicotyledons as well as monocotyledons.

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Section: Storage Proteinssupporting

confidence: 83%

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Thioredoxin-Linked Proteins Are Reduced during Germination ofMedicago truncatulaSeeds

et al. 2007

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“…The difference in the total GSH between crude and supernatant should reflect the amount of GSH bound to insoluble proteins. Because glutelin and polymers are water-insoluble without SDS 11 , they should not be recovered in the supernatant. Table 1 summarizes the quantitative results.…”

Section: Quantitative Analysis Of Glutathionementioning

confidence: 99%

Further Studies on the Protein Chemistry and Property of Glutathione-Added Rice Bread : Evidence of Glutathionylation of Batter Protein as well as Crumb Structure/Sensory Evaluation

Yano

Kaji

Tokuriki

2013

JARQ

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Rice is one of the major staple crops in many developing countries, so commercializing rice-based processed foods should help boost their economy. We have recently reported that the addition of glutathione, a natural ubiquitous tri-peptide, to rice batter allows it to retain the carbon dioxide gas in fermentation, whereupon subsequent baking swells the rice bread without the need for added gluten. Although we have just detected this phenomenon, further mechanical and qualitative investigation should accelerate studies for its practical application. We speculate that the swelling is due to the "barrier theory". In short, disulfide-linked protein polymers hinder the adsorption of water by the starch granules. Glutathione may cleave or hinder the formation of the disulfide bonds of the polymers, which boosts starch hydration, resulting in increased viscosity and continuity of the rice batter. In this paper, we have obtained evidence that glutathione modifies the sulfhydryl groups of the barrier proteins (glutathionylation) and increases their solubility, thus fraying the barrier. Although further studies are needed to reveal the complete swelling mechanism, these observations support and extend the hypothesized barrier-linked swelling mechanism of glutathione bread. Moreover, from a bread quality perspective, the fine/coarse property of crumbs is found to be controllable, and the sensory assessment demonstrated that the bread smell is unimpaired by glutathione. All these data will accelerate the practical use of the glutathione bread.

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“…Rice glutelin exists as large macromolecular complexes formed by disulfide and hydrophobic interactions of acidic and basic chains. Monitoring rice seed germination by the disulfide proteome [57] demonstrated that mobilization of glutelin occurred in an ordered, sequential combination of proteolysis and reduction of disulfide groups. First, limited proteolysis truncated the individual glutelin molecules, thereby disrupting the original rigid hexamer conformation to render the protein more soluble and the disulfide bonds of its fragments accessible to reduction.…”

Section: Disulfide Proteome Analysismentioning

confidence: 99%

Update and challenges on proteomics in rice

Komatsu

Yano

2006

Proteomics

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Rice is not only an important agricultural resource but also a model plant for biological research. Our previous review highlighted different aspects of the construction of rice proteome database, cataloguing rice proteins of different tissues and organelle, differential proteomics using 2-DE and functional characterization of some of the proteins identified (Komatsu, S., Tanaka, N., Proteomics 2005, 5, 938-949). In this review, the powerfulness and weaknesses of proteomic technologies as a whole and limitations of the currently used techniques in rice proteomics are discussed. The information obtained from these techniques regarding proteins modification, protein-protein interaction and the development of new methods for differential proteomics will aid in deciphering more precisely the functions of known and/or unknown proteins in rice.

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Redox Changes Accompanying the Degradation of Seed Storage Proteins in Germinating Rice

Cited by 67 publications

References 24 publications

Thioredoxin-Linked Proteins Are Reduced during Germination ofMedicago truncatulaSeeds

Thioredoxin-Linked Proteins Are Reduced during Germination ofMedicago truncatulaSeeds

Further Studies on the Protein Chemistry and Property of Glutathione-Added Rice Bread : Evidence of Glutathionylation of Batter Protein as well as Crumb Structure/Sensory Evaluation

Update and challenges on proteomics in rice

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