Metabolic Stability of the Two Forms of Initiation Factor IF‐3 in Escherichia coli during the Growth Cycle
- 1 January 1978
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 82 (1), 271-277
- https://doi.org/10.1111/j.1432-1033.1978.tb12020.x
Abstract
Possible alteration in the ratio of the long and short forms of initiation factor IF-3 during the growth cycle of E. coli was examined. The ratio remained unchanged between the exponential and stationary growth phases. Contrary to an earlier report, the total amount of IF-3 relative to the ribosome content in stationary phase cells was essentially the same as in midlog phase cells. The activity of IF-3, assayed after its separation from other initiation factors by chromatography, was also the same in extracts from midlog and stationary phase cells. In E. coli the ratio of IF-3/ribosome is apparently maintained constantly. The ribosomes themselves retained virtually full activity in vitro during this transition indicating that growth-cycle-dependent biochemical modifications of the ribosome do not affect its protein synthetic capacity per se.This publication has 27 references indexed in Scilit:
- The primary structure of the initiation factor IF‐3 from Escherichia coliFEBS Letters, 1977
- Separation of two forms of IF‐3 in Escherichia coli by two‐dimensional gel electrophoresisFEBS Letters, 1977
- Isolation and Characterization of a Growth‐Cycle‐Reflecting, High‐Molecular‐Weight Protein Associated with Escherichia coli RibosomesEuropean Journal of Biochemistry, 1976
- Role of Ribosomal Protein S1 in Protein Synthesis: Effects of Its Addition to Bacillus stearothermophilus Cell‐Free SystemEuropean Journal of Biochemistry, 1975
- Release of 70 S ribosomes from polysomes in Escherichia coliJournal of Molecular Biology, 1973
- Deficiency in Initiation Factors of Protein Synthesis in Stationary‐Phase Escherichia coliEuropean Journal of Biochemistry, 1972
- Defective ribosomes in chloramphenicol-treated Escherichia coliJournal of Molecular Biology, 1971
- Association of polypeptide initiation factors with 30 S ribosomal subunitsFEBS Letters, 1969
- Purification and properties of bacteriophage MS2 and of its ribonucleic acidJournal of Molecular Biology, 1963
- Ribonucleoprotein particles from Escherichia coliJournal of Molecular Biology, 1959