Regulation of protein synthesis in rabbit reticulocyte lysates: purification and initial characterization of the cyclic 3':5'-AMP independent protein kinase of the heme-regulated translational inhibitor.
- 1 December 1976
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 73 (12) , 4349-4353
- https://doi.org/10.1073/pnas.73.12.4349
Abstract
The heme-regulated translational inhibitor (HRI) was purified 4800-fold. On electrophoresis in sodium dodecyl sulfate/polyacrylamide gel, the purified HRI showed 1 major polypeptide band. The purified HRI inhibits protein synthesis in lysates containing optimal levels of hemin with inhibition kinetics which parallel those observed in heme-deficiency. Data are presented which are consistent with an enzymatic function of HRI in the inhibition of protein synthesis. The HRI is cyclic AMP independent protein kinase which phosphorylates the small subunit (38,000) but not the large subunits (52,000 and 50,000) of the initiation factor which forms a ternary complex with Met-tRNAf and GTP. This evidence supports the hypothesis that inhibition of protein synthesis by HRI involves the phosphorylation of the initiation factor. These findings are discussed in relation to various models for the regulation of protein kinase activity by heme. .**GRAPHIC**.This publication has 39 references indexed in Scilit:
- On the mechanism of delayed inhibition of protein synthesis in heme-defecient rabbit reticulocyte lysates.Proceedings of the National Academy of Sciences, 1976
- CONTROL OF GLOBIN SYNTHESISBritish Medical Bulletin, 1976
- Factors involved in initiation of haemoglobin synthesis can be phosphorylated in vitroNature, 1976
- Regulation of protein synthesis in reticulocyte lysates: phosphorylation of methionyl-tRNAf binding factor by protein kinase activity of translational inhibitor isolated from hemedeficient lysates.Proceedings of the National Academy of Sciences, 1976
- Specificity of the protein kinase activity associated with the hemin-controlled repressor of rabbit reticulocyte.Proceedings of the National Academy of Sciences, 1976
- Initiation of Eukaryotic Protein Synthesis: [Met-tRNAf.40S Ribosome] Initiation Complex Catalysed by Purified Initiation Factors in the Absence of mRNANature New Biology, 1973
- Control of Globin Synthesis in Cell-Free Preparations of Reticulocytes by Formation of a Translational Repressor That is Inactivated by HeminProceedings of the National Academy of Sciences, 1972
- Control of globin synthesis: The role of hemeJournal of Molecular Biology, 1972
- The effect of hemin on the synthesis of globinBiochemical and Biophysical Research Communications, 1965
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951