Wheat (Triticum aestivum L.) [gamma]-Gliadin Accumulates in Dense Protein Bodies within the Endoplasmic Reticulum of Yeast

Rosenberg, Nurit; Shimoni, Yuval; Altschuler, Yoram; Levanony, Hanna; Volokita, Micha; Galili, Gad

doi:10.1104/pp.102.1.61

Cited by 30 publications

(21 citation statements)

References 34 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Severa1 lines of evidente have recently shown that a considerable amount of the storage proteins assemble into PB within the ER Galili et al, 1993;Rosenberg et al, 1993). Thus, the presence of ER-resident proteins inside the PB may be due to their trapping inside the storage protein complexes during PB formation within the ER.…”

Section: Lntracellular Localization Of Pdimentioning

confidence: 99%

Purification, Characterization, and Intracellular Localization of Glycosylated Protein Disulfide Isomerase from Wheat Grains

et al. 1995

Self Cite

View full text Add to dashboard Cite

~ ~Wheat (Trificum aestivum) storage proteins fold and assemble into complexes that are linked by intra-and intermolecular disulfide bonds, but it is not yet clear whether these processes are spontaneous or require the assistance of endoplasmic reticulum (ER)-resident enzymes and molecular chaperones. Aiming to unravel these processes, we have purified and characterized the enzyme protein disulfide isomerase (PDI) from wheat endosperm, as well as studied its developmental expression and intracellular localization. This ER-resident enzyme was previously shown to be involved in the formation of disulfide bonds in secretory proteins. Wheat PDI appears as a 60-kD glycoprotein and is among the most abundant proteins within the ER of developing grains. PDI is notably upregulated in developing endosperm in comparison to embryos, leaves, and roots. In addition, the increase in PDI expression in grains appears at relatively early stages of development, preceding the onset of storage protein accumulation by several days. Subcellular localization analysis and immunogold labeling of electron micrographs showed that PDI is not only present in the lumen of the ER but is also co-localized with the storage proteins in the dense protein bodies. These observations are consistent with the hypothesis that PDI is involved in the assembly of wheat storage proteins within the ER.

show abstract

Section: Lntracellular Localization Of Pdimentioning

confidence: 99%

Purification, Characterization, and Intracellular Localization of Glycosylated Protein Disulfide Isomerase from Wheat Grains

et al. 1995

Self Cite

View full text Add to dashboard Cite

show abstract

“…It is interesting to note that the g-gliadin polypeptide was found to be transport competent also when expressed in transgenic tobacco plants (Napier et al, 1997), but it was found to form protein body-like structures in the yeast ER (Rosenberg et al, 1993). The cell type-specific destiny of a g-gliadin when expressed in heterologous systems may reflect differences in the ER machinery or in the concentration reached by the newly synthesized protein in the ER lumen.…”

Section: Protein Bodiesmentioning

confidence: 99%

Protein Quality Control Mechanisms and Protein Storage in the Endoplasmic Reticulum. A Conflict of Interests?

Vitale

Ceriotti

2004

Plant Physiology

View full text Add to dashboard Cite

“…[5][6][7][8]11,19) In addition, rice prolamin has been shown to form ER-derived PBs in plant tissues such as rice leaves, roots, 12) and calli.…”

Section: Discussionmentioning

confidence: 99%

Identification of the region of rice 13 kDa prolamin essential for the formation of ER-derived protein bodies using a heterologous expression system

Masumura

Shigemitsu

Morita

et al. 2015

Bioscience, Biotechnology, and Biochemistry

View full text Add to dashboard Cite

Cereal prolamins, which are alcohol-soluble seed storage proteins, can induce ER-derived protein bodies (PBs) in heterologous tissue. Like maize and wheat prolamins, rice prolamins can form ERderived PBs, but the region of mature polypeptides that is essential for PB formation has not been identified. In this study, we examined the formation mechanisms of ER-derived PB-like structures by expressing rice 13 kDa prolamin-deletion mutants fused to green fluorescent protein (GFP) in heterologous tissues such as yeast. The 13 kDa prolamin-GFP fusion protein was stably accumulated in transgenic yeast and formed an ER-derived PB-like structure. In contrast, rice α-globulin-GFP fusion protein was transported to vacuoles. In addition, the middle and COOH-terminal regions of 13 kDa prolamin formed ER-derived PB-like structures, whereas the NH 2 -terminal region of 13 kDa prolamin did not form such structures. These results suggest that the middle and COOH-terminal regions of 13 kDa prolamin can be retained and thus can induce ER-derived PB in yeast.

show abstract

Wheat (Triticum aestivum L.) [gamma]-Gliadin Accumulates in Dense Protein Bodies within the Endoplasmic Reticulum of Yeast

Cited by 30 publications

References 34 publications

Purification, Characterization, and Intracellular Localization of Glycosylated Protein Disulfide Isomerase from Wheat Grains

Purification, Characterization, and Intracellular Localization of Glycosylated Protein Disulfide Isomerase from Wheat Grains

Protein Quality Control Mechanisms and Protein Storage in the Endoplasmic Reticulum. A Conflict of Interests?

Identification of the region of rice 13 kDa prolamin essential for the formation of ER-derived protein bodies using a heterologous expression system

Contact Info

Product

Resources

About