Replacement of Ribosomal Protein S1 by Interference Factor iα in Ribosomal Binding of Phage MS2 RNA
- 1 December 1974
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 71 (12), 4708-4712
- https://doi.org/10.1073/pnas.71.12.4708
Abstract
The MS2 RNA binding capacity of 30S ribosomal subunits, which is lost when protein S1 is removed, can be restored following incubation with interference factor ialpha and repelleting. Polyacrylamide-agarose gel electrophoresis shows that, under these conditions, a faster moving, non-RNA binding 30S species, which contains no S1, is converted to a slower moving RNA-binding one, having the same mobility as the 30S species that contains protein S1. Factor ialpha binds to single-stranded RNAs in a pattern that closely resembles the RNA binding pattern of initiation factor IF-3.Keywords
This publication has 29 references indexed in Scilit:
- Purification and Properties of Initiation Factor IF-3 from Caulobacter crescentusJournal of Biological Chemistry, 1974
- Purification and properties of two messenger-discriminating species of E. coli initiation factor 3Archives of Biochemistry and Biophysics, 1973
- Polyuridylic acid binding and translating by Escherichia coli ribosomes: Stimulation by Protein 1, inhibition by aurintricarboxylic acidBiochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1972
- Specific inhibitors of MS2 and late T4 RNA translation in E. coliBiochemical and Biophysical Research Communications, 1972
- Cistron Specific Translation Control Protein in Escherichia coliNature New Biology, 1972
- Isolation and Properties of Crystalline Initiation Factor F1 from Escherichia coli RibosomesEuropean Journal of Biochemistry, 1971
- Ribosomal proteins of Escherichia coli. II. Chemical and physical characterization of the 30 S ribosomal proteinsBiochemistry, 1969
- Molecular weight estimation and separation of ribonucleic acid by electrophoresis in agarose-acrylamide composite gelsBiochemistry, 1968
- Ordered state of poly-uridylic acid above room temperatureJournal of Molecular Biology, 1966
- Isolation and Physical Properties of the Ribosomal Ribonucleic Acid of Escherichia coli*Biochemistry, 1965