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Biomedical subjects

M Grunberg-Manago

Publications and source records attributed to M Grunberg-Manago.

At least 127 records · Page 7Linked to original sources

Purification and properties of two initiation factors from Bacillus stearothermophilus.

Two initiation factors have been isolated from the thermophilic bacterium, Bacillus stearothermophilus, and purified to near homogeneity. The two factors possess physical characteristics and activities associated with the E. coli initiation factors IF-2 and IF-3, and are interchangeable with these factors. The two systems present, however, several differences : S-IF-2 is significantly more heat stable than E. coli IF-2, loosing less than 50 per cent of its activity after 20 minutes at 70degreesC. S-IF-2 alone is unable to promote initiation complex formation on B. stearothermophilus or E. coli ribosomes, and S-IF-3 is absolutely necessary for initiation of complex formation on B. stearothermophilus ribosomes. No factor corresponding to IF-1 has been found. S-IF-3 appears to be able to replace at least partially IF-1, since S-IF-3 and E. coli IF-2 are sufficient to promote maximum fMet-tRNA binding to E. coli ribosomes, while E. coli IF-3 and IF-2 also require IF-1. The differences between the two systems are perhaps required because of the elevated temperature at which B. stearothermophilus normally grows.

Amino Acids↗

Implications of electrostatic potentials on ribosomal proteins.

Potentiometric studies of ribosomal particles 30S, 50S, and 70S, were designed to investigate possible implications of the electrostatic potentials developed by the 16S and 23S rRNA fractions. Release of protons and proton titrations of these ribosomal fractions were examined as a function of Mg2+ and K+ concentrations. The effects of these cations fit the polyelectrolyte theory remarkably well and are discussed accordingly.

Bacterial Proteins↗

Stimulation by ATP of protein initiation in a prokaryotic organism, B. stearothermophilus.

In contrast to E. coli ribosomes, with B. stearothermophilus ribosomes initiation complex formation is stimulated by ATP as well as GTP, but maximum stimulation occurs when both the nucleotides are present; and their terminal phosphate must be hydrolysable. In the presence of ATP and GTP, B. stearothermophilus ribosomes synthesize a highly phosphorylated guanine derivative, ppGpp, and the role of ATP in initiation might be related to this synthesis. We discarded the role of ATP as being trivial and corresponding solely to the well-known effect on eukaryotic systems.

Adenosine Triphosphate↗

Ribosomal subunit interaction as studied by light scattering. Evidence of different classes of ribosome preparations.

The Mg2+-dependent equilibrium of ribosomal subunits was studied by light scattering in the absence of any other factor of protein synthesis. The difference of intensity in the light scattered by dissociated 30S-50S couples and by 70S particles was used as a method to measure the percentage of association as a function of Mg2+ under conditions of nonperturbation of the equilibrium. We found that pressure-resistant (type A) and non-pressure-resistant (type B) ribosomes may be characterized by the different behavior of their association equilibrium curves. The thermodynamic parameters of this equilibrium and their comparison for the two classes of ribosomes were calculated from experiments at different temperatures.

Cell Fractionation↗