A conserved motif is essential for the correct assembly of proglutelins and for their export from the endoplasmic reticulum in rice endosperm
| العنوان: | A conserved motif is essential for the correct assembly of proglutelins and for their export from the endoplasmic reticulum in rice endosperm |
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| المؤلفون: | Masako Fukuda, Yanping Xing, Lihong Tian, Le Qing Qu, Rong Li, Toshihiro Kumamaru, Xiangbai Dong, Dandan Qian |
| المصدر: | Journal of Experimental Botany |
| بيانات النشر: | Oxford University Press, 2018. |
| سنة النشر: | 2018 |
| مصطلحات موضوعية: | 0106 biological sciences, 0301 basic medicine, endoplasmic reticulum export, Glutens, Physiology, Immunoelectron microscopy, protein assembly, Sequence alignment, Plant Science, Endoplasmic Reticulum, 01 natural sciences, Conserved sequence, 03 medical and health sciences, Storage protein, Amino Acid Sequence, Disulfide bonds, Peptide sequence, Conserved Sequence, Plant Proteins, chemistry.chemical_classification, rice endosperm, Base Sequence, Endoplasmic reticulum, Oryza, Cell Biology, Research Papers, Endosperm, Cell biology, Amino acid, 030104 developmental biology, chemistry, sequence motif, Sequence motif, glutelin, Sequence Alignment, 010606 plant biology & botany |
| الوصف: | Characterization of a mutant that specifically accumulates the GluA precursor reveals a conserved motif in proglutelins that is essential for their proper assembly in, and their subsequent export from, the endoplasmic reticulum. Rice glutelins are initially synthesized as 57-kDa precursors at the endoplasmic reticulum (ER) and are ultimately transported into protein storage vacuoles. However, the sequence motifs that affect proglutelin folding, assembly, and their export from the ER remain poorly defined. In this study, we characterized a mutant with nine amino acids deleted in the GluA2 protein, which resulted in specific accumulation of the GluA precursor. The deleted amino acids constitute a well-conserved sequence (LVYIIQGRG) in glutelins and all residues in this motif are necessary for ER export of GluA2. Immunoelectron microscopy and stable transgenic analyses indicated that proglutelins with deletion of this motif misassembled and aggregated through non-native intermolecular disulfide bonds, and were deposited in ER-derived protein bodies (PB-Is), resulting in conversion of PB-Is into a new type of PB. These results indicate that the conserved motif is essential for proper assembly of proglutelin. The correct assembly of proglutelins is critical for their segregation from prolamins in the ER lumen, which is essential for enabling the export of proglutelin from the ER and for the proper formation of PB-Is. We also found that the interchain disulfide bond between acidic and basic subunits is not necessary for their assembly, but it is required for proglutelin folding. |
| اللغة: | English |
| تدمد: | 1460-2431 0022-0957 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bda0235ed65bf69819f536121df7621d http://europepmc.org/articles/PMC6184509 |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....bda0235ed65bf69819f536121df7621d |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 14602431 00220957 |
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