Coexpression of the maize delta-zein and beta-zein genes results in stable accumulation of delta-zein in endoplasmic reticulum-derived protein bodies formed by beta-zein.

Bagga, Suman; Adams, H. R.; Rodriguez, Fabian D.; Kemp, John D.; Sengupta‐Gopalan, Champa

doi:10.1105/tpc.9.9.1683

Cited by 71 publications

(43 citation statements)

References 35 publications

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“…It is possible that the proteins in this group all have a function in ER-derived protein body formation. Experiments that involved the transgenic expression of zeins in tobacco (Nicotiana tabacum) showed that ER-localized protein bodies can form, at least temporarily, in dicotyledons (Bagga et al, 1995(Bagga et al, , 1997Coleman et al, 1996Coleman et al, , 2004, and it is tempting to speculate that this is also possible in Arabidopsis. The group of proteins that are characterized by the presence of a signal peptide could function in protein scaffolding processes in other parts of the secretory system.…”

Section: Discussionmentioning

confidence: 99%

The Maize Floury1 Gene Encodes a Novel Endoplasmic Reticulum Protein Involved in Zein Protein Body Formation

et al. 2007

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The maize (Zea mays) floury1 (fl1) mutant was first reported almost 100 years ago, but its molecular identity has remained unknown. We report the cloning of Fl1, which encodes a novel zein protein body membrane protein with three predicted transmembrane domains and a C-terminal plant-specific domain of unknown function (DUF593). In wild-type endosperm, the FL1 protein accumulates at a high level during the period of zein synthesis and protein body development and declines to a low level at kernel maturity. Immunogold labeling showed that FL1 resides in the endoplasmic reticulum surrounding the protein body. Zein protein bodies in fl1 mutants are of normal size, shape, and abundance. However, mutant protein bodies ectopically accumulate 22-kD a-zeins in the g-zein-rich periphery and center of the core, rather than their normal discrete location in a ring at outer edge of the core. The 19-kD a-zein is uniformly distributed throughout the core in wildtype protein bodies, and this distribution is unaffected in fl1 mutants. Pairwise yeast two-hybrid experiments showed that FL1 DUF593 interacts with the 22-kD a-zein. Results of these studies suggest that FL1 participates in protein body formation by facilitating the localization of 22-kD a-zein and that this is essential for the formation of vitreous endosperm.

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Section: Discussionmentioning

confidence: 99%

The Maize Floury1 Gene Encodes a Novel Endoplasmic Reticulum Protein Involved in Zein Protein Body Formation

et al. 2007

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“…Therefore, g-and b-zeins are not required for the normal accumulation of a-and d-zeins in maize endosperm. This was rather unexpected because in heterologous systems like tobacco (Nicotiana tabacum), a-and d-zeins could never accumulate at high levels unless they were coexpressed with the 27-kD g-or b-zein (Coleman et al, 1996;Bagga et al, 1997).…”

Section: Analysis Of the New Set Of Transgenic Seeds And Their Crossesmentioning

confidence: 99%

“…Expression of zeins in heterologous systems has been thought of as a test case for genetic engineering of nutritionally improved seeds. But when an attempt was made to express single a-or d-zein gene copies in tobacco endosperm, zein proteins failed to accumulate unless coexpressed with g-or b-zein (Coleman et al, 1996(Coleman et al, , 2004Bagga et al, 1997;Hinchliffe and Kemp, 2002). These findings indicated that a-zein or d-zein in tobacco was prone to degradation and that coexpression of Cys-rich g-or b-zein, which could initiate protein body formation alone, stabilized a-or d-zein by sequestering them into protein bodies.…”

Section: Need Of Homologous Expression Systems To Validate Gene Functionmentioning

confidence: 99%

RNA Interference-Mediated Change in Protein Body Morphology and Seed Opacity through Loss of Different Zein Proteins

2010

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Opaque or nonvitreous phenotypes relate to the seed architecture of maize (Zea mays) and are linked to loci that control the accumulation and proper deposition of storage proteins, called zeins, into specialized organelles in the endosperm, called protein bodies. However, in the absence of null mutants of each type of zein (i.e. a, b, g, and d), the molecular contribution of these proteins to seed architecture remains unclear. Here, a double null mutant for the d-zeins, the 22-kD a-zein, the b-zein, and the g-zein RNA interference (RNAi; designated as z1CRNAi, bRNAi, and gRNAi, respectively) and their combinations have been examined. While the d-zein double null mutant had negligible effects on protein body formation, the bRNAi and gRNAi alone only cause slight changes. Substantial loss of the 22-kD a-zeins by z1CRNAi resulted in protein body budding structures, indicating that a sufficient amount of the 22-kD zeins is necessary for maintenance of a normal protein body shape. Among different mutant combinations, only the combined bRNAi and gRNAi resulted in drastic morphological changes, while other combinations did not. Overexpression of a-kafirins, the homologues of the maize 22-kD a-zeins in sorghum (Sorghum bicolor), in the b/gRNAi mutant failed to offset the morphological alterations, indicating that b-and g-zeins have redundant and unique functions in the stabilization of protein bodies. Indeed, opacity of the b/gRNAi mutant was caused by incomplete embedding of the starch granules rather than by reducing the vitreous zone.

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“…Previous studies investigating the heterologous expression of zein subgroups alone or in combination have shown that the presence and balanced interaction of all zein subfamilies is necessary to stabilize the zein bodies and form typical spherical structures. Thus, although δ-zein [42], β-zein (re-assigned to the γ-zein subfamily [31]) [43], and γ-zein [28] can form protein aggregates by themselves, these do not form typical zein bodies. For example, α-zein forms stable protein bodies when expressed in Xenopus laevis oocytes but not in tobacco leaves, but typical protein body structures are formed ectopically when different zein subtypes are coexpressed [44].…”

Section: Insoluble 2g12 Accumulates Due To Covalent Interactions Withmentioning

confidence: 92%

Efficient recovery of recombinant proteins from cereal endosperm is affected by interaction with endogenous storage proteins

Peters

Sabalza

Ramessar

et al. 2013

Biotechnology Journal

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Cereal seeds are versatile platforms for the production of recombinant proteins because they provide a stable environment for protein accumulation. Endogenous seed storage proteins, however, include several prolamin-type polypeptides that aggregate and crosslink via intermolecular disulfide bridges, which could potentially interact with multimeric recombinant proteins such as antibodies, which assemble in the same manner. We investigated this possibility by sequentially extracting a human antibody expressed in maize endosperm, followed by precipitation in vitro with zein. We provide evidence that a significant proportion of the antibody pool interacts with zein and therefore cannot be extracted using non-reducing buffers. Immunolocalization experiments demonstrated that antibodies targeted for secretion were instead retained within zein bodies because of such covalent interactions. Our findings suggest that the production of soluble recombinant antibodies in maize could be enhanced by eliminating or minimizing interactions with endogenous storage proteins.

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Coexpression of the maize delta-zein and beta-zein genes results in stable accumulation of delta-zein in endoplasmic reticulum-derived protein bodies formed by beta-zein.

Cited by 71 publications

References 35 publications

The Maize Floury1 Gene Encodes a Novel Endoplasmic Reticulum Protein Involved in Zein Protein Body Formation

The Maize Floury1 Gene Encodes a Novel Endoplasmic Reticulum Protein Involved in Zein Protein Body Formation

RNA Interference-Mediated Change in Protein Body Morphology and Seed Opacity through Loss of Different Zein Proteins

Efficient recovery of recombinant proteins from cereal endosperm is affected by interaction with endogenous storage proteins

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