PMID: 19567376 BiP 浼翠荆铔嬬櫧 鍐呰川缃戝簲婵 璐瓨铔嬬櫧
Plant Cell Physiol. 2009 Aug
Overexpression of BiP has inhibitory effects on the accumulation of seed storage proteins in endosperm cells of rice聽 [涓嬭浇]
璐棌铔嬬櫧鍦ㄧ瀛愭垚鐔熻繃绋嬩腑鐗瑰紓澶ч噺鍚堟垚骞剁粡鐢卞唴璐ㄧ綉娌夌Н鍦ㄨ泲鐧戒綋锛圥B锛夊唴锛岃繖涓绉嶇Н绱繃绋嬬敱ER浼翠荆濡侭iP锛孭DI绛変粙瀵笺備负浜嗙爺绌惰繖浜涗即渚h泲鐧界殑浣滅敤鍜屽畠浠笌绉嶅瓙璐棌铔嬬櫧绉疮姘村钩鍙樺寲涔嬮棿鐨勮仈绯伙紝浠ヨ儦涔崇壒寮傚惎鍔ㄥ瓙glutelin promoter鍦ㄦ鏍儦涔充腑杩囪〃杈綛ip鍜孭DI銆侾DI杩囪〃杈炬鏍殑琛ㄥ瀷鍜學T宸笉澶氾紝浣咮ip杩囪〃杈炬鏍憟鐜颁笉閫忔槑锛屽叿浣撹〃鍨嬩负绮夎川floury鍜岀毐缂﹕hrink锛岃串钘忚泲鐧藉拰娣绮夊惈閲忕殑姘村钩閮戒綆浜嶹T銆傛湁瓒g殑鏄紝鍦ㄨ浆鍖栨牚涓紝涓嶅厜鏉ヨ嚜ER鐨凱B-I鏋勫瀷鏀瑰彉锛岃屼笖杩樹骇鐢熶簡鏂扮殑绫籔B缁撴瀯锛岃缁撴瀯鍖呮嫭BiP锛屽惈璋疯泲鐧界殑楂樼數瀛愬瘑搴﹀熀璐ㄥ拰鍚胺閱囨憾铔嬬櫧鐨勪綆鐢靛瓙瀵嗗害鍩鸿川锛屽苟涓旇繕闄勭潃澶氭牳绯栦綋锛岀爺绌舵帹娴嬭繖绫绘瀯鍨嬪彲鑳藉睘浜嶦R浜х敓鐨凱B-I鐨勮鐢熺墿锛屽畠浜х敓浜庡唴璐ㄧ綉锛屽苟瀵圭瀛愯泲鐧界殑缈昏瘧锛屾姌鍙犲拰浼犻佹湁鎶戝埗浣滅敤銆
Seed storage proteins are specifically and highly synthesized during seed maturation and are deposited into protein bodies (PBs) via the endoplasmic reticulum (ER) lumen. The accumulation process is mediated by ER chaperones such as luminal binding protein (BiP) and protein disulfi de isomerase (PDI). To examine the role of ER chaperones and the relationship between ER chaperones and levels of
accumulation of seed storage proteins, we generated transgenic rice plants in which the rice BiP and PDI genes were overexpressed in an endosperm-specifi c manner under the control of the rice seed storage protein glutelin promoter. The seed phenotype of the PDI overexpressing transformant was almost identical to that of the wild type, whereas overexpression of BiP resulted in transgenic rice seed that displayed an opaque phenotype with floury and shrunken features. In the BiP-overexpressing line, the levels of accumulation of seed storage proteins and starch contents were signifi cantly lower compared with the wild type. Interestingly, overproduction of BiP in the endosperm of the transformant not only altered the morphological
structure of ER-derived PB-I, but also generated unusual new PB-like structures composed of a high electron density matrix containing glutelin and BiP and a low electron density matrix containing prolamins. Notably, polysomes were attached around the aberrant PB-like structures, indicating that this aberrant structure is an ER-derived
PB-I derivative. These results suggested that the PB-like structure may be formed in the ER lumen, resulting in inhibition of translation, folding and transport of seed proteins.

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