Introduction of the Disulfide Proteome: Application of a Technique for the Analysis of Plant Storage Proteins as Well as Allergens

Yano, Hiroyuki; Kuroda, S.

doi:10.1021/pr8003453

Cited by 19 publications

(13 citation statements)

References 76 publications

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“…It is evident from the study of their structures that disulfide bond reduction would reduce the compact folding of these storage proteins. In fact, the redox state within the PSV contributes to the regulation of storage protein degradation, illustrated in wheat (Wong et al 2004), barley (Shahpiri et al 2008) and rice (Yano and Kuroda 2008). In rice, limited proteolysis of the acidic chains of the glutelins is followed by reduction of the disulfide bonds linking the acidic to the basic chain, making the modified storage protein more accessible to subsequent rapid extensive proteolysis.…”

Section: Pathways Of Breakdown Of Other Storage Proteinsmentioning

confidence: 99%

Mobilization of seed protein reserves

Tan-Wilson

Wilson

2011

Physiologia Plantarum

175

109

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The mobilization of seed storage proteins upon seed imbibition and germination is a crucial process in the establishment of the seedling. Storage proteins fold compactly, presenting only a few vulnerable regions for initial proteolytic digestion. Evolutionarily related storage proteins have similar three-dimensional structure, and thus tend to be initially cleaved at similar sites. The initial cleavage makes possible subsequent rapid and extensive breakdown catalyzed by endo- and exopeptidases. The proteolytic enzymes that degrade the storage proteins during mobilization identified so far are mostly cysteine proteases, but also include serine, aspartic and metalloproteases. Plants often ensure early initiation of storage protein mobilization by depositing active proteases during seed maturation, in the very compartments where storage proteins are sequestered. Various means are used in such cases to prevent proteolytic attack until after imbibition of the seed with water. This constraint, however, is not always enforced as the dry seeds of some plant species contain proteolytic intermediates as a result of limited proteolysis of some storage proteins. Besides addressing fundamental questions in plant protein metabolism, studies of the mobilization of storage proteins will point out proteolytic events to avoid in large-scale production of cloned products in seeds. Conversely, proteolytic enzymes may be applied toward reduction of food allergens, many of which are seed storage proteins.

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Section: Pathways Of Breakdown Of Other Storage Proteinsmentioning

confidence: 99%

Mobilization of seed protein reserves

Tan-Wilson

Wilson

2011

Physiologia Plantarum

175

109

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“…As discussed in our previous review 54 , molecular specificity and expression patterns are important determinants of Trx-target specificity. In brief, site-directed mutagenesis studies 36 suggested that electrostatic interactions between Trx and target induced the following formation of their non-covalent binary complex.…”

Section: Current Challengesmentioning

confidence: 94%

“…Moreover, the knowledge obtained will be useful in developing new variety of plants/crops with improved yield, disease-resistance and cultivation suitability which should benefit developing countries. In medical studies, this knowledge may also reveal important clues to understand the mecha-JARQ 46 (4) 2012 T. Kawakami & H. Yano seed biochemistry 54 as well as food allergens 53 has been summarized in recent reviews. A comprehensive list of putative targets, as of 2009, is also available 35 .…”

Section: Introductionmentioning

confidence: 99%

Disulfide Proteomics: Current Status in Thioredoxin Biochemistry and Industrial Research

Kawakami¹,

Yano

2012

JARQ

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nisms of various human diseases and, more practically, to identify potential drug targets and biomarkers.In 2001, the concept of proteomics has been incorporated into Trx-linked studies. Yano et al. 57 and Motohashi et al. 37 independently developed major proteomic approaches based on discrete principles. The affinity column strategy 37 allows the concentration of the targets, while the fluorescent gel approach 57 is applicable to both in vitro and in vivo analyses. These two methods, with their improved versions, have since been applied to elucidate Trx-linked biochemistry 26 , and the number of putative targets has reached 400 35 . Following a brief introduction of these two basic methods, the present short review focuses on the recent advancement of a technique that can effectively tackle problems such as target authenticity. The review also introduces two industrial research areas, food processing and medical investigation, in which proteomic studies are underway. Proteomic approaches to identify Trx targetsIn this section, basic proteomic methods are briefly introduced, while application of the techniques to plant IntroductionPost-translational modification (PTM) functions in a broad spectrum of biology. Among the regulatory mechanisms involved, reversible protein phosphorylation has been most widely studied and developing the phosphoproteomics technique has enhanced our understanding of this mode of regulation. Meanwhile, a growing body of evidence suggests that reversible reduction/oxidation (redox) of protein disulfide bonds regulates critical processes in all cell types 12 . Thioredoxins (Trxs) are small (10-14 kDa), widely distributed redox proteins involved in the regulation of numerous target proteins via thiol/disulfide exchanges, and thus play key roles in maintaining cellular redox homeostasis 34,44 . Thus, a better understanding of redox biology could be achieved if more were known about their target proteins. Moreover, the knowledge obtained will be useful in developing new variety of plants/crops with improved yield, disease-resistance and cultivation suitability which should benefit developing countries. In medical studies, this knowledge may also reveal important clues to understand the mecha-JARQ 46 (4), 277 -285 (2012) AbstractRedox regulation is a central control element across a broad spectrum of biology. Thioredoxin (Trx), a widely distributed disulfide enzyme, participates in the control of numerous target proteins, thus playing a key role in regulatory processes. Identification of Trx's targets will therefore aid the elucidation of redox biology. Two recently developed procedures, one based on thiol-specific probes and the other on affinity trapping, have facilitated the labeling or isolation of potential Trx targets that were later identified with proteomic approaches. Accordingly, the number of identified targets in plants has increased to 400. This review describes recent advances in proteomic strategies that are effectively overcoming challenging problems such as the evaluation ...

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“…I t i s a n important factor for stabilizing the protein conformation. In addition, oxidation-reduction of Cys residues in protein is significant to biological functions (Lee et al, 2004;Mieyal et al, 2008;Yano & Kuroda, 2008). Therefore, the assignment of disulfide bonding patterns will not only provide insights into its threedimensional structure and contribute to the understanding of its structure-function relationship but will also play a role in the regulation of fundamental cellular processes.…”

Section: In Addition It I S P O S S I B L E T H a T O U R M S S Y S mentioning

confidence: 99%