Evidence for a second phosphorylation site on eIF‐2α from rabbit reticulocytes

FEBS Letters

Kudlicki, Wieslaw²  Kemp, Bruce E.¹  Hardesty, Boyd²  Kramer, Gisela²  Szyszka, Ryszard²  Wettenhall, Richard E.H.³ 

[1] Department of Medicine, University of Melbourne, Repatriation General Hospital, Heidelberg, Victoria 3081, Australia;Clayton Foundation Biochemical Institute and Department of Chemistry, University of Texas, Austin, TX 78712, USA;Department of Biochemistry, La Trobe University, Bundoora, Victoria 3083, Australia

关键词: Protein synthesis;    Peptide initiation;    Protein kinase;    Phosphorylation site;    Amino acid sequence;    eIF-2a;    α-subunit of eukaryotic initiation factor 2;    HPLC;    high-performance liquid chromatography;    TFA;    trifluoroacetic acid;   

DOI  :  10.1016/0014-5793(87)80105-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Ser 51 in the NH₂-terminal sequence of the α-subunit of eukaryotic peptide initiation factor 2 (eIF-2) has been identified as a second phosphorylation site for the heme-controlled eIF-2α kinase from rabbit reticulocytes. Increased phosphorylation of this serine relative to the previously described phosphorylation site (Ser 48) is observed when the kinase reaction is carried out in the presence of the α-subunit of spectrin. A synthetic peptide corresponding to eIF-2α(41–54) is phosphorylated only in Ser 51 by the eIF-2α kinase.

【 授权许可】

Unknown