Abstract
Ribosomes of the extreme thermophilic hydrogen-oxidizing bacterium Calderobacterium hydrogenophilum interact with a broad spectrum of polyamines. In the absence of polyamines and at 70°C close to the growth optimum (75°C), high salt washed ribosomes lost their activity in the poly(UG)-directed polypeptide synthesis. At 70°C the in vitro system synthesized the polypeptide in the presence of spermidine, spermine or natural polyamines (tri-pentaamines) isolated from ribosomal extracts but not in the presence of putrescine. The activity of ribosomes was affected by a number of antibiotics interfering with functions of typical eubacterial 70S, such as tetracyclines, lincomycin, chloramphenicol and erythromycin. However, the ribosomes were relatively resistant to streptomycin and insensitive to 80S inhibitors, such as ricin and cycloheximide. The 30S and 50S subunits have structural features typical of eubacterial ribosomes.
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The authors dedicated this paper to Professor Ivan Málek on the occasion of his 80th birthdy to remember his contribution to the Czechoslovak microbiology
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Mikulík, K., Jiráňová, A., Maňas, J. et al. Polypeptide synthesis on ribosomes of an extreme thermophilic hydrogen bacterium Calderobacterium hydrogenophilum . Arch. Microbiol. 153, 248–253 (1990). https://doi.org/10.1007/BF00249076
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DOI: https://doi.org/10.1007/BF00249076