Regulation of protein synthesis in rabbit reticulocyte lysates

FEBS Letters

Singh Ranu, Rajinder¹ 

[1] Department of Microbiology, Colorado State University, Fort Collins, CO 80523, USA

关键词: Heme-regulated protein kinase Initiation factor eIF-2 Protein synthesis Phosphorylation Thiophosphorylation;   

DOI  :  10.1016/0014-5793(86)81544-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The heme-regulated protein kinase, which specifically phosphorylates the 38-kDa subunit of initiation factor eiF-2, can utilize adenosine 5′-O-(3-thiotriphosphate) (ATP[γS]) as a substrate. The rate of thiophosphorylation is 5-6-times slower than that observed with ATP. It is of special interest that thiophosphorylated derivatives of eIF-2 are resistant to dephosphorylation catalyzed by eIF-2 phosphoprotein phosphatase. The thiophosphorylated eIF-2 is less effective in promoting protein synthesis in hemin-deficient lysates under physiological conditions. In addition, ATP[γS] could also be utilized by the self-phosphorylation activity intrinsically associated with HRI.

【 授权许可】

Unknown