RICE PROLAMINE PROTEIN BODY BIOGENESIS - A BIP-MEDIATED PROCESS
RICE PROLAMINE PROTEIN BODY BIOGENESIS - A BIP-MEDIATED PROCESS
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DOI：
10.1126/science.8235623
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发表时间：
1993-11-12
期刊：
影响因子：
56.9
通讯作者：
OKITA, TW
中科院分区：
文献类型：
--
作者：
LI, XX;WU, YJ;OKITA, TW
水稻醇溶蛋白被隔离在内质网（ER）腔内，即使他们缺乏内腔滞留信号。免疫化学和生物化学数据表明，BiP，一种结合内腔多肽的蛋白质，位于聚集的醇溶谷蛋白体（PB）的表面上。BiP还与多聚核糖体中的醇溶谷蛋白的新生链和具有不同的三磷酸腺苷敏感性的游离醇溶谷蛋白形成复合物。因此，BiP通过促进其折叠和组装成PB而将醇溶谷蛋白保留在管腔中。
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.