Inhibition of protein synthesis in rabbit reticulocyte lysates by double-stranded RNA and oxidized glutathione: indirect mode of action on polypeptide chain initiation.
- 1 April 1975
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 72 (4), 1286-1290
- https://doi.org/10.1073/pnas.72.4.1286
Abstract
In the presence of added double-stranded RNA or oxidized glutathione, protein synthesis in heminsupplemented reticulocyte lysates declines abruptly after 8-12 min of incubation at 30 degrees. The kinetics of amino-acid incorporation are very similar to those seen when lysates incorporation are very similar to those seen when lysates are incubated in the absence of added hemin. The inhibitory effects of double-stranded RNA (dsRNA) and oxidized glutathione (GSSG) are partially overcome by a homogeneous initiation factor, IF-MP, which also stimulates protein synthesis in hemin-deficient lysates. This factor is involved in the binding of Met-tRNAfmet to 40S ribosomal subunits during protein chain initiation. However, neither dsRNA alone nor GSSG alone significantly inhibits formation of [40S subunit-Met-tRNAf] complexes induced in reticulocyte lysates by dsRNA or GSSG involves one or more components present in the lysates but absent from the fractionated in vitro system. Such components may be related to the translational inhibitor that is active in hemin-deficient lysates.Keywords
This publication has 23 references indexed in Scilit:
- Met-tRNA f Met Binding to 40S Ribosomal Subunits: A Site for the Regulation of Initiation of Protein Synthesis by HeminProceedings of the National Academy of Sciences, 1974
- The Effects of Hemin and Double-Stranded RNA on α and β Globin Synthesis in Reticulocyte and Krebs II Ascites Cell-Free Systems and the Relationship of These Effects to an Initiation Factor PreparationProceedings of the National Academy of Sciences, 1974
- 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
- Translation of Exogenous Messenger RNA for Hemoglobin on Reticulocyte and Liver RibosomesProceedings of the National Academy of Sciences, 1971
- Inhibition of Peptide Initiation on Reticulocyte Ribosomes by EdeineEuropean Journal of Biochemistry, 1971
- Hemin control of globin synthesis: An assay for the inhibitor formed in the absence of hemin and some characteristics of its formationJournal of Molecular Biology, 1971
- Studies on cessation of protein synthesis in a reticulocyte lysate cell-free systemBiochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1970
- Stimulation of globin-chain initiation by hemin in the reticulocyte cell-free system.Proceedings of the National Academy of Sciences, 1968