Rice prolamin species form a layered structure in the protein body type I (PB-I) storage organelle. Rice prolamins are classified as 10 kDa, 13a-1, 13a-2, 13b-1, 13b-2 and 16 kDa prolamin. Prolamin species form layer structure in PB-I in order of 10 kDa core, 13b-1 layer, 13a (13a-1 and 13a-2) and 16 kDa middle layer and 13b-2 outer-most layer. In a previous study, we showed that the fusion proteins in 13b-2 prolamin-GFP, 13a-1 prolamin-GFP and 10 kDa prolamin-GFP were localized in the same layer of PB-I as the native prolamin, when they were expressed by their respective native prolamin promoters. Our preliminary study suggested that the temporal control of the native prolamin promoters was responsible for the localization of the respective prolamins. The aim of this study was to determine whether the use of a prolamin promoter other than the native prolamin promoter would change the localization of prolamin-GFP fusion proteins. For this purpose, we generated transgenic lines expressing 13b-2 prolamin-GFP and 13a-1 prolamin-GFP fusion proteins driven by each prolamin promoter other than the native prolamin promoter. As a result, the localization of the fusion protein in PB-I was changed. Based on our results, foreign protein localization in PB-I can be achieved by the temporal control of the different prolamin promoters.
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http://dx.doi.org/10.5511/plantbiotechnology.18.0918a | DOI Listing |
Plant Foods Hum Nutr
January 2025
Laboratorio de Investigación en Funcionalidad y Tecnología de Alimentos (LIFTA), Departamento de Ciencia y Tecnología, Universidad Nacional de Quilmes, Bernal, Argentina.
Quinoa flour due to its nutritional and sensory characteristics could be used as an ingredient to improve the nutritional and technological properties of gluten-free bread. Furthermore, the application of hydrothermal processes such as extrusion can enhance their native properties. Hence, our objective was to evaluate how the incorporation of extruded quinoa flours (EQFs) affects the technological, sensory and nutritional quality of gluten-free bread.
View Article and Find Full Text PDFFood Chem
February 2025
College of Food Science and Engineering, Qingdao Agricultural University, Qingdao 266109, People's Republic of China. Electronic address:
A simple and efficient one-step method combining ion crosslinking and antisolvent exchange has been developed to construct gellan gum/corn starch@zein (GG/CS@Z) core-shell structured beads. This novel approach aims to reduce the digestibility and digestion rate of starch. The GG/CS@Z beads were comprehensively characterized using scanning electron microscopy (SEM), confocal laser scanning microscope (CLSM), differential scanning calorimetry (DSC), swelling power experiments and in vitro simulated digestion tests, respectively.
View Article and Find Full Text PDFJ Food Sci
November 2024
Department of Natural Sciences (DCN), State University of the Southwest of Bahia (UESB), Vitória da Conquista, Bahia, Brazil.
Cytokine
October 2024
Institute of Food Sciences, CNR, via Roma 64, 83100 Avellino, Italy.
We have previously shown the ability of transamidated gluten (spf) to modulate both innate and adaptive intestinal immunity elicited by wheat gliadin in HLA-DQ8 transgenic mice (DQ8 mice), a model of gluten sensitivity. Herein, we evaluated the influence of spf when administered intragastrically on the immune response to native gliadin in DQ8 mice. To address the issue, we analysed three regimens of antigen administration: before immunisation (pre-treatment), during immunisation (co-treatment) and through breast milk during the lactating phase (suckling treatment).
View Article and Find Full Text PDFNature
August 2024
Division of Hematology, Department of Medicine, Stanford University School of Medicine, Stanford, CA, USA.
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