ArticleJournal of experimental botany2018
Maize 16-kD γ-zein forms very unusual disulfide-bonded polymers in the endoplasmic reticulum: implications for prolamin evolution.
Article in Journal of experimental botany, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 18 citations in OpenAlex.
- Molecular characterization, haplotype analysis and development of markers specific to3 Biotech · 2024Article
- Generation of multi-layered protein bodies inFrontiers in plant science · 2023Article
- Specialized endoplasmic reticulum-derived vesicles in plants: Functional diversity, evolution, and biotechnological exploitation.Journal of integrative plant biology · 2022Review
- Confocal Fluorescence Microscopy Investigation for the Existence of Subdomains within Protein Storage Vacuoles in Soybean Cotyledons.International journal of molecular sciences · 2022Article
- StresSeed: The Unfolded Protein Response During Seed Development.Frontiers in plant science · 2022Review
- Cell Biology Methods to Study Recombinant Proteins in Seeds.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Progressive Aggregation of 16 kDa Gamma-Zein during Seed Maturation in TransgenicInternational journal of molecular sciences · 2021Article
- 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
- Methods for the Modification and Evaluation of Cereal Proteins for the Substitution of Wheat Gluten in Dough Systems.Foods (Basel, Switzerland) · 2021Review
- Variations in Amino Acid and Protein Profiles in White versus Brown Teff (Foods (Basel, Switzerland) · 2019Article
- NAC-type transcription factors regulate accumulation of starch and protein in maize seeds.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Russell-Like Bodies in Plant Seeds Share Common Features With Prolamin Bodies and Occur Upon Recombinant Protein Production.Frontiers in plant science · 2019Article
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
Abstract
In the lumen of the endoplasmic reticulum (ER), prolamin storage proteins of cereal seeds form very large, ordered heteropolymers termed protein bodies (PBs), which are insoluble unless treated with alcohol or reducing agents. In maize PBs, 16-kD γ-zein locates at the interface between a core of alcohol-soluble α-zeins and the outermost layer mainly composed of the reduced-soluble 27-kD γ-zein. 16-kD γ-zein originates from 27-kD γ-zein upon whole-genome duplication and is mainly characterized by deletions in the N-terminal domain that eliminate most Pro-rich repeats and part of the Cys residues involved in inter-chain bonds. 27-kD γ-zein also forms insoluble PBs when expressed in transgenic vegetative tissues. We show that in Arabidopsis leaves, 16-kD γ-zein assembles into disulfide-linked polymers that fail to efficiently become insoluble. Instead of forming PBs, these polymers accumulate as very unusual threads that markedly enlarge the ER lumen, resembling amyloid-like fibers. Domain-swapping between the two γ-zeins indicates that the N-terminal region of 16-kD γ-zein has a dominant effect in preventing full insolubilization. Therefore, a newly evolved prolamin has lost the ability to form homotypic PBs, and has acquired a new function in the assembly of natural, heteropolymeric PBs.
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