CYTOPLASMIC PROTEIN BINDS INVITRO TO A HIGHLY CONSERVED SEQUENCE IN THE 5-SUBUNIT UNTRANSLATED REGION OF FERRITIN HEAVY-SUBUNIT AND LIGHT-SUBUNIT MESSENGER-RNAS
CYTOPLASMIC PROTEIN BINDS INVITRO TO A HIGHLY CONSERVED SEQUENCE IN THE 5-SUBUNIT UNTRANSLATED REGION OF FERRITIN HEAVY-SUBUNIT AND LIGHT-SUBUNIT MESSENGER-RNAS
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DOI：
10.1073/pnas.85.7.2171
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发表时间：
1988-04-01
影响因子：
11.1
通讯作者：
MUNRO, HN
中科院分区：
文献类型：
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作者：
LEIBOLD, EA;MUNRO, HN
铁储存蛋白铁蛋白的重亚基和轻亚基的mRNA在细胞中主要以无活性的核糖核蛋白颗粒的形式存在，当铁进入细胞时，这些颗粒被募集用于翻译。从大鼠组织和肝癌细胞的胞质提取物显示通过电泳分离程序形成RNA-蛋白质复合物，其涉及铁蛋白重亚基和轻亚基mRNA的5“非翻译区中的高度保守序列。复合物形成的模式受到预处理的大鼠或细胞与铁。通过UV irradation交联显示，复合物含有与铁蛋白mRNA的保守序列相互作用的87-kDa蛋白。我们提出，细胞内铁水平调节铁蛋白的合成引起的变化，在特定的蛋白结合的铁蛋白重和轻亚基mRNA的保守序列。
The mRNAs for the heavy and light subunits of the iron-storage protein ferritin occur in cells largely as inactive ribonucleoprotein particles, which are recruited for translation when iron enters the cell. Cytoplasmic extracts from rat tissues and hepatoma cells were shown by an electrophoretic separation procedure to form RNA-protein complexes involving a highly conserved sequence in the 5'' untranslated region of both ferritin heavy- and light-subunit mRNAs. The pattern of complex formation was affected by pretreatment of rats or cells with iron. Crosslinking by UV irradation showed that the complexes contained an 87-kDa protein interacting with the conserved sequence of the ferritin mRNA. We propose that intracellular iron levels regulate ferritin synthesis by causing changes in specific protein binding to the conserved sequence in the ferritin heavy- and light-subunit mRNAs.