Relationship between Endogenous Protein Disulfide Isomerase Family Proteins and Glutenin Macropolymer

Koh, Akie; Nishimura, Kimio; Urade, Reiko

doi:10.1021/jf103347p

Cited by 20 publications

(13 citation statements)

References 36 publications

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“…Because wheat flour arises from milled starchy endosperm, the five groups of PDI family proteins must be present in flour (Table 4). We previously detected oxidative refolding activity in an extract from wheat flour, and its activity was inhibited by the PDI inhibitor bacitracin [66]. Therefore, PDI family proteins may be active in both the starchy endosperm of the dry mature grain and flour.…”

Section: Resultsmentioning

confidence: 99%

“…Furthermore, PDI family proteins may affect the quality of food products. We previously demonstrated that PDI family proteins play a role in retaining glutenin macropolymers during dough mixing, and these polymers are the most important factor for dough’s tensile strength [66]. We semi-quantitatively analyzed the levels of the five PDI family protein groups in a wheat flour sample (Table 4) and found that among the five groups of PDI family proteins, TaPDIL1 levels were the highest.…”

Section: Resultsmentioning

confidence: 99%

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Expression and characterization of protein disulfide isomerase family proteins in bread wheat

et al. 2015

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BackgroundThe major wheat seed proteins are storage proteins that are synthesized in the rough endoplasmic reticulum (ER) of starchy endosperm cells. Many of these proteins have intra- and intermolecular disulfide bonds. In eukaryotes, the formation of most intramolecular disulfide bonds in the ER is thought to be catalyzed by protein disulfide isomerase (PDI) family proteins. The cDNAs that encode eight groups of bread wheat (Triticum aestivum L.) PDI family proteins have been cloned, and their expression levels in developing wheat grains have been determined. The purpose of the present study was to characterize the enzymatic properties of the wheat PDI family proteins and clarify their expression patterns in wheat caryopses.ResultsPDI family cDNAs, which are categorized into group I (TaPDIL1Aα, TaPDIL1Aβ, TaPDIL1Aγ, TaPDIL1Aδ, and TaPDIL1B), group II (TaPDIL2), group III (TaPDIL3A), group IV (TaPDIL4D), and group V (TaPDIL5A), were cloned. The expression levels of recombinant TaPDIL1Aα, TaPDIL1B, TaPDIL2, TaPDIL3A, TaPDIL4D, and TaPDIL5A in Escherichia coli were established from the cloned cDNAs. All recombinant proteins were expressed in soluble forms and purified. Aside from TaPDIL3A, the recombinant proteins exhibited oxidative refolding activity on reduced and denatured ribonuclease A. Five groups of PDI family proteins were distributed throughout wheat caryopses, and expression levels of these proteins were higher during grain filling than in the late stage of maturing. Localization of these proteins in the ER was confirmed by fluorescent immunostaining of the immature caryopses. In mature grains, the five groups of PDI family proteins remained in the aleurone cells and the protein matrix of the starchy endosperm.ConclusionsHigh expression of PDI family proteins during grain filling in the starchy endosperm suggest that these proteins play an important role in forming intramolecular disulfide bonds in seed storage proteins. In addition, these PDI family proteins that remain in the aleurone layers of mature grains likely assist in folding newly synthesized hydrolytic enzymes during germination.Electronic supplementary materialThe online version of this article (doi:10.1186/s12870-015-0460-2) contains supplementary material, which is available to authorized users.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Expression and characterization of protein disulfide isomerase family proteins in bread wheat

et al. 2015

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“…The most thoroughly characterized to date involves oxidation of substrate proteins by protein disulfide isomerase (PDI), which is in turn oxidized by the endoplasmic reticulum oxidase Ero1, which was first identified in yeast (Frand and Kaiser, ; Pollard et al ., ). It has recently been shown that plant homologues of Ero1 and PDI are also involved in storage protein deposition in rice (Onda et al ., , ; Satoh‐Cruz et al ., ), and that PDI plays an important role in glutenin polymerization during the breadmaking process (Koh et al ., ). However, the pathways that mediate disulfide bond formation within the plant ER have not been characterized in detail.…”

Section: Introductionmentioning

confidence: 97%

Redox regulation of glutenin subunit assembly in the plant endoplasmic reticulum

et al. 2012

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SUMMARYThe glutenin fraction of wheat storage proteins consists of large polymers in which high-and low-molecularweight subunits are connected by inter-chain disulfide bonds. We found that assembly of a low-molecularweight glutenin subunit in the endoplasmic reticulum is a rapid process that leads to accumulation of various oligomeric forms, and that this assembly is sensitive to perturbation of the cellular redox environment. In endoplasmic reticulum-derived microsomes, low-molecular-weight glutenin subunits are subjected to hyperpolymerization, indicating that cytosolic factors play an important role in limiting polymer size. Addition of physiological concentrations of reduced glutathione is sufficient to maintain the original polymerization pattern of the glutenin subunits upon cytosol dilution. Furthermore, we show that a low-molecular-weight glutenin subunit can be glutathionylated in endoplasmic reticulum-derived microsomes, and that it can be directly reduced by glutathione in vitro. These results indicate that glutenin polymerization is sensitive to changes in the redox state of the cell, and suggest that the presence of a reducing cytosolic environment plays an important role in regulating disulfide bond formation in the endoplasmic reticulum of plant cells.

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“…LMW-GS are encoded by Glu-A3, Glu-B3 and Glu-D3 loci on the short arms of group 1 chromosomes (GUPTA and SHEPHERD, 1990), which are further divided into B-, C-and D-group subunits according to their mobilities in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) (D'OVIDIO and MASCI, 2004). HMW-GS contain 4-7 cysteine residues and LMW-GS have six conserved cysteine residues and one or more additional cysteine residues (KOH et al, 2010). Most of these residues form intrachain disulfide bonds, whereas some of these residues form interchain disulfide bonds to form GMPs (ORSI, 2001).…”

Section: Introductionmentioning

confidence: 99%

Effects of glu-1 and glu-3 allelic variations on wheat glutenin macropolymer (GMP) content as revealed by size-exclusion high performance liquid chromatography (SE-HPLC)

et al. 2017

Genetika

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2017): Effects of glu-1 and glu-3 allelic variations on wheat glutenin macropolymer (GMP) content as revealed by size-exclusion high performance liquid chromatography vol 49, no. 2,(677)(678)(679)(680)(681)(682)(683)(684)(685)(686)(687)(688)(689)(690)(691) Gluten macropolymers (GMPs), formed by seed storage proteins glutenins and gliadins through intermolecular disulfide bond, confer dough viscoelasticity and wheat processing quality. Glutenins consist of high and low molecular weight glutenin subunits (HMW-GS, LMW-GS) encoded by Glu-1 and Glu-3 loci, respectively. The allelic variations at both loci have important effects on GMP content and breadmaking quality. In this study, GMP extraction and size-exclusion high performance liquid chromatography (SE-HPLC) separation were optimized, and then applied to investigate the effects of Glu-1 and Glu-3 allelic variations on GMP content using different wheat genotypes, chromosome 678 GENETIKA, Vol. 49, No.2, 677-691, 2017 substitution lines and near-isogenic lines (NILs). The results showed that the optimized GMP extraction and SE-HPLC protocol could obtain a reproducible separation and reliable quantitation of GMP content with small samples. The allelic variations at Glu-1 and Glu-3 were closely related to GMP content. Particularly, Glu-D1d encoded 1Dx5+1Dy10 subunits, Glu-A3a and Glu-B3h encoded an abundant LMW-B subunit respectively had positive effects on GMP content and breadmaking quality. The introgress of HMW-GS and LMW-GS into bread wheat from related genomes could significantly increase GMP content, indicating that wheat related species has potential gene resources for breadmaking quality improvement. Our results demonstrated that SE-HPLC could serve as an effective tool for rapid separation and quantitation of GMPs and had potential application for gluten quality screening in the early generations during wheat quality improvement program.

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Relationship between Endogenous Protein Disulfide Isomerase Family Proteins and Glutenin Macropolymer

Cited by 20 publications

References 36 publications

Expression and characterization of protein disulfide isomerase family proteins in bread wheat

Expression and characterization of protein disulfide isomerase family proteins in bread wheat

Redox regulation of glutenin subunit assembly in the plant endoplasmic reticulum

Effects of glu-1 and glu-3 allelic variations on wheat glutenin macropolymer (GMP) content as revealed by size-exclusion high performance liquid chromatography (SE-HPLC)

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