Regulation of binding of initiator tRNA to eukaryotic initiation factor eIF‐2

FEBS Letters

Proud, Christopher G.²  Clemens, Michael J.¹  Pain, Virginia M.² 

[1] Department of Biochemistry, St. George's Hospital Medical School, Cranmer Terrace, London, SW17 ORE, England;School of Biological Sciences, University of Sussex, Falmer, Brighton, BN1 9QG England

关键词: Protein synthesis;    Reticulocyte lysate;    Eukaryotic initiation factor-2;    eIF-2;    eukaryotic initiation factor-2;    HCR;    haem-controlled repressor;    Hepes;    4-(2-hydroxyethyl)-1-piperazine sulphonic acid;   

DOI  :  10.1016/0014-5793(82)80810-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Ternary complex formation was studied in reticulocyte lysate supernatants and using rat liver eukaryotic initiation factor-2 (eIF-2) preparations. Haem-deficiency reduced the rate of formation of ternary (Met-tRNA_f · GTP · eIF-2) complexes by the eIF-2 in reticulocyte supernatants, the reduction being more marked when complex formation was assayed in the absence of GTP-regenerating capacity. Pretreatment with the haem-controlled repressor (HCR) reduced the rate of ternary complex formation by crude (liver) eIF-2. In contrast, complex formation by an almost homogeneous eIF-2 preparation was unaffected by HCR: sensitivity to HCR was however restored by a factor which catalyses exchange of guanine nucleotides bound to eIF-2.

【 授权许可】

Unknown