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大鼠肝脏中的pp49蛋白可与蛋白激酶CK2形成复合物,它由翻译起始因子eIF-2的β亚基和γ亚基组成。

Rat liver pp49, a protein that forms complexes with protein kinase CK2, is composed of the beta and the gamma subunits of translation initiation factor eIF-2.

作者信息

Gil C, Plana M, Riera M, Itarte E

机构信息

Departament de Bioquímica i de Biologia Molecular, Universitat Autònoma de Barcelona, Bellaterra, Spain.

出版信息

Biochem Biophys Res Commun. 1996 Aug 23;225(3):1052-7. doi: 10.1006/bbrc.1996.1293.

Abstract

Comparison of the amino acid sequences of two peptides derived from proteolysis of rat liver pp49 identified it as composed of the beta-subunit and the gamma-subunit of eukaryotic initiation factor-2 (eIF-2). Partial purification of rat liver eIF-2 showed that its trimeric form (alpha beta gamma) co-eluted with protein kinase CK2. Heat-inactivated preparations of the trimeric form of eIF-2 inhibited CK2, increasing its Km for beta-casein, as observed with pp49. The form of eIF-2 that lacks the beta-subunit had no effect on CK2. These data indicate that the beta gamma subunits of eIF-2 may complex with CK2 and modulate its activity.

摘要

对源自大鼠肝脏pp49蛋白水解的两种肽的氨基酸序列进行比较后,确定其由真核生物起始因子2(eIF-2)的β亚基和γ亚基组成。大鼠肝脏eIF-2的部分纯化表明,其三聚体形式(αβγ)与蛋白激酶CK2共同洗脱。eIF-2三聚体形式的热失活制剂抑制CK2,增加其对β-酪蛋白的Km值,正如pp49所观察到的那样。缺乏β亚基的eIF-2形式对CK2没有影响。这些数据表明,eIF-2的βγ亚基可能与CK2结合并调节其活性。

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