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Updated: Jun 22, 2026

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Published on: November 28, 2025
Expression of unprocessed glutelin precursor alters polymerization without affecting trafficking and accumulation
Yuhya Wakasa1, Lijun Yang, Sakiko Hirose
1Transgenic Crop Research and Development Center, National Institute of Agrobiological Sciences, Kannondai 3-1-3, Tsukuba, Ibaraki 305-8604, Japan.
Rice glutelin post-translational processing is not essential for protein body targeting. However, this processing is crucial for forming the higher-order structure necessary for proper glutelin assembly and stacking in protein bodies.
Area of Science:
- Plant molecular biology
- Protein biochemistry
- Seed storage proteins
Background:
- Rice glutelin, a major seed storage protein, is synthesized as a precursor.
- It undergoes post-translational processing and forms aggregates in protein body-II (PB-II).
- The functional role of this processing in folding and assembly remains unclear.
Purpose of the Study:
- To investigate the functional role of glutelin post-translational processing.
- To determine its effect on folding and assembly within protein bodies.
- To analyze the impact of a mutation at the processing site on glutelin deposition.
Main Methods:
- Expressed wild-type GluA2 and a mutant GluA2 (mGluA2) lacking the processing site in transgenic rice.
- Utilized endosperm-specific promoter (GluB1) in a glutelin-deficient rice line (a123).
- Analyzed protein targeting, processing, assembly, and complex formation in PB-II.
Main Results:
- mGluA2 precursor was synthesized, targeted to PB-II, and stably accumulated without processing.
- Unprocessed mGluA2 precursor formed trimers with processed glutelin GluB, unlike processed GluA2.
- mGluA2 precursor formed distinct complexes in PB-II compared to processed GluA2.
Conclusions:
- Post-translational processing of rice glutelin is not required for its trafficking and accumulation in PB-II.
- Processing is essential for the formation of higher-order structures needed for proper glutelin stacking in PB-II.
- This processing influences hetero-assembly with other glutelin types.
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