内质网
生物发生
细胞生物学
蛋白质折叠
三磷酸腺苷
分泌蛋白
化学
折叠(DSP实现)
管腔(解剖学)
生物化学
生物
分泌物
基因
电气工程
工程类
作者
Xingxiang Li,Yujia Wu,Dianzhong Zhang,Jeffrey W. Gillikin,Rebecca S. Boston,Vincent R. Franceschi,Thomas W. Okita
出处
期刊:Science
[American Association for the Advancement of Science (AAAS)]
日期:1993-11-12
卷期号:262 (5136): 1054-1056
被引量:173
标识
DOI:10.1126/science.8235623
摘要
Rice prolamines are sequestered within the endoplasmic reticulum (ER) lumen even though they lack a lumenal retention signal. Immunochemical and biochemical data show that BiP, a protein that binds lumenal polypeptides, is localized on the surface of the aggregated prolamine protein bodies (PBs). BiP also forms complexes with nascent chains of prolamines in polyribosomes and with free prolamines with distinct adenosine triphosphate sensitivities. Thus, BiP retains prolamines in the lumen by facilitating their folding and assembly into PBs.
科研通智能强力驱动
Strongly Powered by AbleSci AI