Small GTPase Sar1 is crucial for proglutelin and α-globulin export from the endoplasmic reticulum in rice endosperm

Rice seed storage proteins glutelin and α-globulin are synthesized in the endoplasmic reticulum (ER) and deposited in protein storage vacuoles (PSVs). Sar1, a small GTPase, acts as a molecular switch to regulate the assembly of coat protein complex II, which exports secretory protein from the ER to...

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Veröffentlicht in:Journal of experimental botany. - 1985. - 64(2013), 10 vom: 15. Juli, Seite 2831-45
1. Verfasser: Tian, Lihong (VerfasserIn)
Weitere Verfasser: Dai, Ling Ling, Yin, Zhi Jie, Fukuda, Masako, Kumamaru, Toshihiro, Dong, Xiang Bai, Xu, Xiu Ping, Qu, Le Qing
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2013
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Endoplasmic reticulum OsSar1 protein body protein intracellular transport protein storage vacuole rice storage proteins. Alpha-Globulins Plant Proteins mehr... Protein Precursors Glutens 8002-80-0 Monomeric GTP-Binding Proteins EC 3.6.5.2
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520 |a Rice seed storage proteins glutelin and α-globulin are synthesized in the endoplasmic reticulum (ER) and deposited in protein storage vacuoles (PSVs). Sar1, a small GTPase, acts as a molecular switch to regulate the assembly of coat protein complex II, which exports secretory protein from the ER to the Golgi apparatus. To reveal the route by which glutelin and α-globulin exit the ER, four putative Sar1 genes (OsSar1a/b/c/d) were cloned from rice, and transgenic rice were generated with Sar1 overexpressed or suppressed by RNA interference (RNAi) specifically in the endosperm under the control of the rice glutelin promoter. Overexpression or suppression of any OsSar1 did not alter the phenotype. However, simultaneous knockdown of OsSar1a/b/c resulted in floury and shrunken seeds, with an increased level of glutelin precursor and decreased level of the mature α- and β-subunit. OsSar1abc RNAi endosperm generated numerous, spherical, novel protein bodies with highly electron-dense matrixes containing both glutelin and α-globulin. Notably, the novel protein bodies were surrounded by ribosomes, showing that they were derived from the ER. Some of the ER-derived dense protein bodies were attached to a blebbing structure containing prolamin. These results indicated that OsSar1a/b/c play a crucial role in storage proteins exiting from the ER, with functional redundancy in rice endosperm, and glutelin and α-globulin transported together from the ER to the Golgi apparatus by a pathway mediated by coat protein complex II 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 4 |a Endoplasmic reticulum 
650 4 |a OsSar1 
650 4 |a protein body 
650 4 |a protein intracellular transport 
650 4 |a protein storage vacuole 
650 4 |a rice storage proteins. 
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650 7 |a Plant Proteins  |2 NLM 
650 7 |a Protein Precursors  |2 NLM 
650 7 |a Glutens  |2 NLM 
650 7 |a 8002-80-0  |2 NLM 
650 7 |a Monomeric GTP-Binding Proteins  |2 NLM 
650 7 |a EC 3.6.5.2  |2 NLM 
700 1 |a Dai, Ling Ling  |e verfasserin  |4 aut 
700 1 |a Yin, Zhi Jie  |e verfasserin  |4 aut 
700 1 |a Fukuda, Masako  |e verfasserin  |4 aut 
700 1 |a Kumamaru, Toshihiro  |e verfasserin  |4 aut 
700 1 |a Dong, Xiang Bai  |e verfasserin  |4 aut 
700 1 |a Xu, Xiu Ping  |e verfasserin  |4 aut 
700 1 |a Qu, Le Qing  |e verfasserin  |4 aut 
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856 4 0 |u http://dx.doi.org/10.1093/jxb/ert128  |3 Volltext 
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