Regulation of protein synthesis in rabbit reticulocyte lysates. Requirement of initiation factor eIF-2 holoprotein for substrate specificity of heme-regulated protein kinase.
Regulation of protein synthesis in rabbit reticulocyte lysates. Requirement of initiation factor eIF-2 holoprotein for substrate specificity of heme-regulated protein kinase.
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兔网织红细胞裂解物中蛋白质合成的调节。
DOI：
10.1016/0014-5793(86)81103-6
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发表时间：
1986
期刊：
影响因子：
3.5
通讯作者：
Ranu,RS
中科院分区：
文献类型：
--
作者：
Roberts,RC;Ranu,RS
通过利用分离的eIF-2的38000 Da亚基（α亚基）多肽作为底物，进一步研究了血红素调节蛋白激酶（HRI）的特异性。为此，通过反相高效液相色谱法（HPLC）分离eIF-2的三个亚基多肽（38000 Da，α，50000 Da，β和52000 Da，γ）。结果显示，HRI不能磷酸化与其他两种eIF-2多肽分离的38000 Da亚基。数据表明，HRI的底物特异性是由eIF-2全蛋白中α亚基与其他两个亚基结合的四级结构决定的。
The specificity of the heme‐regulated protein kinase (HRI) was investigated further by utilizing the isolated 38000 Da subunit (α subunit) polypeptide of eIF‐2 as the substrate. For this purpose, the three subunit polypeptides of eIF‐2 (38000 Da, α, 50000 Da, β; and 52000 Da, γ) were resolved by reversed‐phase high performance liquid chromatography (HPLC). Results show that HRI is incapable of phosphorylating the 38000 Da subunit separated from the other two eIF‐2 polypeptides. Data suggest that the substrate'specificity of HRI is determined by the quaternary structure assumed by the α subunit in association with the other two subunits in the eIF‐2 holoprotein.