ArticlePlant physiology2004
Zeolin. A new recombinant storage protein constructed using maize gamma-zein and bean phaseolin.
Article in Plant physiology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed, 112 citations in OpenAlex.
- Article
- Nano-bio-encapsulation of phyto-vaccines: a breakthrough in targeted cancer immunotherapy.Molecular biology reports · 2024Review
- Protein Biosynthesis and Maturation in the ER.Methods in molecular biology (Clifton, N.J.) · 2024Article
- OverexpressingInternational journal of molecular sciences · 2023Article
- Generation of multi-layered protein bodies inFrontiers in plant science · 2023Article
- Towards microalga-based superfoods: heterologous expression of zeolin inFrontiers in plant science · 2023Article
- Genetic and molecular understanding for the development of methionine-rich maize: a holistic approach.Frontiers in plant science · 2023Review
- Maximizing the Production of Recombinant Proteins in Plants: From Transcription to Protein Stability.International journal of molecular sciences · 2022Review
- Specialized endoplasmic reticulum-derived vesicles in plants: Functional diversity, evolution, and biotechnological exploitation.Journal of integrative plant biology · 2022Review
- Two γ-zeins induce the unfolded protein response.Plant physiology · 2021Article
- Elastin-like polypeptide and γ-zein fusions significantly increase recombinant protein accumulation in soybean seeds.Transgenic research · 2021Article
- Genetic engineering to improve essential and conditionally essential amino acids in maize: transporter engineering as a reference.Transgenic research · 2021Article
- 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
- The Unfolded Protein Response Supports Plant Development and Defense as well as Responses to Abiotic Stress.Frontiers in plant science · 2017Review
- Overexpression of the olive acyl carrier protein gene (OeACP1) produces alterations in fatty acid composition of tobacco leaves.Transgenic research · 2016Article
- Where do Protein Bodies of Cereal Seeds Come From?Frontiers in plant science · 2016Review
- A Fusion between Domains of the Human Bone Morphogenetic Protein-2 and Maize 27 kD γ-Zein Accumulates to High Levels in the Endoplasmic Reticulum without Forming Protein Bodies in Transgenic Tobacco.Frontiers in plant science · 2016Article
- The Encapsulation of Hemagglutinin in Protein Bodies Achieves a Stronger Immune Response in Mice than the Soluble Antigen.Frontiers in plant science · 2016Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The major seed storage proteins of maize (Zea mays) and bean (Phaseolus vulgaris), zein and phaseolin, accumulate in the endoplasmic reticulum (ER) and in storage vacuoles, respectively. We show here that a chimeric protein composed of phaseolin and 89 amino acids of gamma-zein, including the repeated and the Pro-rich domains, maintains the main characteristics of wild-type gamma-zein: It is insoluble unless its disulfide bonds are reduced and forms ER-located protein bodies. Unlike wild-type phaseolin, the protein, which we called zeolin, accumulates to very high amounts in leaves of transgenic tobacco (Nicotiana tabacum). A relevant proportion of the ER chaperone BiP is associated with zeolin protein bodies in an ATP-sensitive fashion. Pulse-chase labeling confirms the high affinity of BiP to insoluble zeolin but indicates that, unlike structurally defective proteins that also extensively interact with BiP, zeolin is highly stable. We conclude that the gamma-zein portion is sufficient to induce the formation of protein bodies also when fused to another protein. Because the storage proteins of cereals and legumes nutritionally complement each other, zeolin can be used as a starting point to produce nutritionally balanced and highly stable chimeric storage proteins.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.