GTP interacts through its ribose and phosphate moieties with different subunits of the eukaryotic initiation factor eIF‐2

FEBS Letters

Kurzchalia, Teymuras V.¹  Bommer, Ulrich-Axel¹ 

[1] Central Institute of Molecular Biology, Academy of Sciences of the GDR, Department of Cell Physiology, Robert-Roessle-Strasse 10, DDR-1115 Berlin-Buch, GDR

关键词: Photoaffinity labeling;    Eukaryotic initiation factor eIF-2;    GTP binding;   

DOI  :  10.1016/0014-5793(89)80555-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We have previously shown that a GTP derivative bearing p-azidoaniline at the γ-phosphate group specifically labels the γ-subunit of eukaryotic initiation factor eIF-2. In the present study a new GTP derivative carrying the photoreactive group at the ribose moiety of GTP was applied for affinity labeling of eIF-2 in different initiation complexes. Using this GTP analogue the β-subunit of eIF-2 was found to be specifically labeled in all complexes investigated. It is concluded that GTP interacts with both the β- and γ-subunit of eIF-2: the guanosine moiety is in contact with the β-subunit and the γ-phosphate group with the γ-subunit.

【 授权许可】

Unknown