ArticleThe Journal of biological chemistry2010
Relevant elements of a maize gamma-zein domain involved in protein body biogenesis.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 55 citations in OpenAlex.
- Article
- Bio-encapsulation of allergen-derivatives for specific immunotherapy.Frontiers in plant science · 2025Article
- Advances in Subcellular Accumulation Design for Recombinant Protein Production in Tobacco.Biodesign research · 2024Review
- Towards microalga-based superfoods: heterologous expression of zeolin inFrontiers in plant science · 2023Article
- Maximizing the Production of Recombinant Proteins in Plants: From Transcription to Protein Stability.International journal of molecular sciences · 2022Review
- Increasing the Efficiency of the Accumulation of Recombinant Proteins in Plant Cells: The Role of Transport Signal Peptides.Plants (Basel, Switzerland) · 2022Review
- Specialized endoplasmic reticulum-derived vesicles in plants: Functional diversity, evolution, and biotechnological exploitation.Journal of integrative plant biology · 2022Review
- Wheat α-gliadin and high-molecular-weight glutenin subunit accumulate in different storage compartments of transgenic soybean seed.Transgenic research · 2022Article
- Two γ-zeins induce the unfolded protein response.Plant physiology · 2021Article
- Review
- Glyco-Engineering of Plant-Based Expression Systems.Advances in biochemical engineering/biotechnology · 2021Article
- Plant-derived protein bodies as delivery vehicles for recombinant proteins into mammalian cells.Biotechnology and bioengineering · 2020Article
- 3D Electron Microscopy Gives a Clue: Maize Zein Bodies Bud From Central Areas of ER Sheets.Frontiers in plant science · 2020Article
- Advances in Plant-Derived Scaffold Proteins.Frontiers in plant science · 2020Review
- Characterization and Immunogenicity of HIV Envelope gp140 ZeraFrontiers in bioengineering and biotechnology · 2020Article
- Russell-Like Bodies in Plant Seeds Share Common Features With Prolamin Bodies and Occur Upon Recombinant Protein Production.Frontiers in plant science · 2019Article
- Maize 16-kD γ-zein forms very unusual disulfide-bonded polymers in the endoplasmic reticulum: implications for prolamin evolution.Journal of experimental botany · 2018Article
- Protein bodies: how the ER deals with high accumulation of recombinant proteins.Plant biotechnology journal · 2017Article
- Development of plant-produced protein body vaccine candidates for bluetongue virus.BMC biotechnology · 2017Article
- Comprehensive proteomic analysis of developing protein bodies in maize (Zea mays) endosperm provides novel insights into its biogenesis.Journal of experimental botany · 2016Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The N-terminal proline-rich domain of γ-zein (Zera) plays an important role in protein body (PB) formation not only in the original host (maize seeds) but in a broad spectrum of eukaryotic cells. However, the elements within the Zera sequence that are involved in the biogenesis of PBs have not been clearly identified. Here, we focused on amino acid sequence motifs that could be involved in Zera oligomerization, leading to PB-like structures in Nicotiana benthamiana leaves. By using fusions of Zera with fluorescent proteins, we found that the lack of the repeat region (PPPVHL)(8) of Zera resulted in the secretion of the fusion protein but that this repeat by itself did not form PBs. Although the repeat region containing eight units was the most efficient for Zera self-assembly, shorter repeats of 4-6 units still formed small multimers. Based on site-directed mutagenesis of Zera cysteine residues and analysis of multimer formation, we conclude that the two N-terminal Cys residues of Zera (Cys(7) and Cys(9)) are critical for oligomerization. Immunoelectron microscopy and confocal studies on PB development over time revealed that early, small, Zera-derived oligomers were sequestered in buds along the rough ER and that the mature size of the PBs could be attained by both cross-linking of preformed multimers and the incorporation of new chains of Zera fusions synthesized by active membrane-bound ribosomes. Based on these results and on the behavior of the Zera structure determined by molecular dynamics simulation studies, we propose a model of Zera-induced PB biogenesis.
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