PROTEIN-SYNTHESIS IN RABBIT RETICULOCYTES - PURIFICATION AND PROPERTIES OF AN MR 80,000 POLYPEPTIDE (CO-EIF-2A80) WITH CO-EIF-2A ACTIVITY
- 1 January 1985
- journal article
- research article
- Vol. 260 (11) , 6945-6949
Abstract
The high MW protein complex, Co-eIF-2 [eukaryotic initiation factor 2 complex], contains both Co-eIF-2A and Co-eIF-2C activities. Co-eIF-2A stimulated Met-tRNAf binding to eukaryotic initiation factor-2 (eIF-2) both in the presence and absence of Mg2+. Co-eIF-2C stimulates Met-tRNAf binding to eIF-2 in the presence of Mg2+ by relieving Mg2+ inhibition of ternary complex formation from eIF-2. Co-eIF-2 protein complex contains several polypeptides including MW 80,000 and 50,000 polypeptides. Three polypeptides (MW 80,000, 50,000 and 25,000) are present in 0.5 M KCl ribosomal salt wash and each possesses Co-eIF-2A activity. MW 80,000 polypeptide (Co-eIF-2A80) has been purified to homogeneity and its properties studied. Co-eIF-2A80 stimualted Met-tRNAf binding to eIF-2 and the complex formed was resistant to aurintricarboxylic acid. Co-eIF-2A80 activity was N-ethylmaleimide-resistant and heat-labile; it was destroyed by heating at 55.degree. C for 4 min. Antibodies prepared against homogeneous Co-eIF-2A80 strongly inhibited protein synthesis is reticulocyte lysates and, also, eIF-2 and Co-eIF-2 promoted Met-tRNAf binding to 40 S ribosomes. Inhibition of protein synthesis in reticulocyte lysates was overcome by preincubation of anti-Co-eIF-2A80 with homogeneous Co-eIF-2A80 and was partially overcome by similar preincubation with Co-eIF-2. Upon limited digestion with Staphylococcus aureus V8 protease, the homogeneous Co-eIF-2A80 gave 2 major polypeptide fragments (MW 50,000 and 25,000). Upon similar treatment, an MW 80,000 polypeptide band isolated from the sodium dodecyl sulfate-gel of the Co-eIF-2 protein complex gave 4 major polypeptide fragments, and 2 of these fragments (MW 50,000 and 25,000) were similar to those given by Co-eIF-2A80, indicating that this MW 80,000 polypeptide band contains the Co-eIF-2A80 component. Co-eIF-2A80 is a component of Co-eIF-2 and is also essential for Co-eIF-2 activity and overall peptide chain initiation.This publication has 28 references indexed in Scilit:
- Protein synthesis in rabbit reticulocytes. Demonstration of the requirements for eIF-2 and Co-eIF-2A for peptide chain initiation using immune sera.Journal of Biological Chemistry, 1979
- Protein synthesis in rabbit reticulocytes: characteristics of a postribosomal supernatant factor that reverses inhibition of protein synthesis in heme-deficient lysates and inhibition of ternary complex (Met-tRNAfMet.eIF-2.GTP) formation by heme-regulated inhibitor.Proceedings of the National Academy of Sciences, 1979
- Protein synthesis in rabbit reticulocytes: mechanism of protein synthesis inhibition by heme-regulated inhibitor.Proceedings of the National Academy of Sciences, 1979
- Purification and Characterization of a Protein Factor that Reverses the Inhibition of Protein Synthesis by the Heme‐Regulated Translational Inhibitor in Rabbit Reticulocyte LysatesEuropean Journal of Biochemistry, 1979
- Regulation of protein synthesis in rabbit reticulocyte lysates: Additional initiation factor required for formation of ternary complex (eIF-2·GTP·Met-tRNA f ) and demonstration of inhibitory effect of heme-regulated protein kinaseProceedings of the National Academy of Sciences, 1979
- PROTEIN-SYNTHESIS IN RABBIT RETICULOCYTES-XXI - PURIFICATION AND PROPERTIES OF A PROTEIN FACTOR (CO-EIF-1) WHICH STIMULATES MET-TRANSFER-RNAF BINDING TO EIF-11978
- Protein synthesis initiation in eucaryotic cells: A comparative study of the mechanism of peptide chain initiation using cell-free systems from mouse ascites tumor cells and rabbit reticulocytesArchives of Biochemistry and Biophysics, 1977
- Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis.Journal of Biological Chemistry, 1977
- Control of protein synthesis by hemin. Isolation and characterization of a supernatant factor from rabbit reticulocyte lysateBiochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1976
- PROTEIN-SYNTHESIS IN RABBIT RETICULOCYTES .14. CHARACTERISTICS OF MESSENGER-RNA (AUG CODON)-DEPENDENT BINDING OF MET-TRANSFER-RNAFMET TO 40 S AND 80 S RIBOSOMES1976