Article
The highly acidic C-terminal region of the yeast initiation factor subunit 2 alpha (eIF-2 alpha) contains casein kinase phosphorylation sites and is essential for maintaining normal regulation of GCN4.
Biochimica et biophysica acta - 26 Apr 1995
van den Heuvel J, Lang V, Richter G, Price N, Peacock L, Proud C, McCarthy J E
Abstract excerpt
Regulation of the effective activity of eukaryotic initiation factor 2 (eIF-2) in protein synthesis is known to involve phosphorylation of its alpha subunit. Two mammalian enzymes, the haem-controlled repressor (HCR) and the double-stranded RNA-activated inhibitor (dsI), phosphorylate Ser-51 of t...
Topics
- Amino Acid Sequence
- Binding Sites
- Casein Kinases
- DNA-Binding Proteins
- Escherichia coli
- Eukaryotic Initiation Factor-2
- Fungal Proteins
- Gene Deletion
- Molecular Sequence Data
- Mutation
- Phosphorylation
- Protein Kinases
- Recombinant Proteins