The enzymic synthesis of aminoacyl derivatives of soluble ribonucleic acid from Bacillus stearothermophilus

Arcà, M.; Calvori, C.; Frontali, Laura; Tecce, G.

doi:10.1016/0926-6550(64)90116-1

Cited by 7 publications

(6 citation statements)

References 21 publications

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“…In agreement with the work of Teece and his coworkers (2,16,28) with another thermophilic bacterium, the differences, if any, in the gross properties of the RNA species present in B. stearothermophilus and E. coli are slight and probably could not account for the increased stability of the protein-synthesizing system. Therefore, the more stable ribosomes of the thermophile may reflect a difference in the ribosomal protein of Bacillus stearothermophilus ribosomes SAUNDERS AND CAMPBELL moiety.…”

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confidence: 87%

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Ribonucleic Acid and Ribosomes of Bacillus stearothermophilus

Saunders

Campbell

1966

J Bacteriol

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SAUNDERS, GRADY F. (University of Illinois, Urbana), AND L. LEON CAMPBELL. Ribonucleic acid and ribosomes of Bacillus stearothermophilus. J. Bacteriol. 91:332-339. 1966.-The ability of some thermophilic bacteria to grow at temperatures as high as 76 C emphasizes the remarkable thermal stability of their crucial macromolecules. An investigation of the ribonucleic acid (RNA) and ribosomes of Bacillus stearothermophilus was conducted. Washed log-phase cells were disrupted either by sonic treatment or by alumina grinding in 10-2 M MgCl2-1(t2 M tris-(hydroxymethyl)aminomethane buffer, pH 7.4 (TM buffer). Ultracentrifugal analysis revealed peaks at 72.5S, lOlS, and 135S, with the lOlS peak being the most prominent. By lowering the Mg++ concentration to 10-M, the ribosome preparation was dissociated to give 40S, 31S, and 54S peaks. These in turn were reassociated in the presence of 102 M Mg++ to give the larger 73S and 135S particles. When heated in TM buffer, Escherichia coli ribosomes began a gradual dissociation at 58 C, and at 70 C underwent a large hyperchromic shift with a Tm at 72.8 C. In contrast, B. stearothermophilus ribosomes did not show a hyperchromic shift below 70 C; they had a Tm of 77.9 C. The thermal denaturation curves of the 4S, 16S, and 23S RNA from both organisms were virtually identical. The gross amino acid composition of B. stearothermophilus ribosomes showed no marked differences from that reported for E. coli ribosomes. These data suggest that the unusual thermal stability of B. stearothermophilus ribosomes may reflect either an unusual packing arrangement of the protein to the RNA or differences in the primary structure of the ribosomal proteins.

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“…Friedman and Weinstein (7) reported that a subcellular amino acid-incorporating system from B. stearothermophilus is active at 65 C. Studies on the ribosomes and ribonucleic acid (RNA) of a thermophilic bacterium (2,16,28) suggest that RNA has a higher thermal stability within the ribosome than in its isolated state.…”

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confidence: 99%

Ribonucleic Acid and Ribosomes of Bacillus stearothermophilus

Saunders

Campbell

1966

J Bacteriol

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“…Aminoacyl sRNA synthetases of B. stearothermophilus were shown to be more heat-stable than the comparable enzymes from E. coli (3,8). The present study compares the ribosomes and ribosomal ribonucleic acid (rRNA) from B. stearothermophilus to those from E. coli and the effects of polyamines on their thermostability.…”

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confidence: 96%

“…2Present address: Department of Biological Sciences, Hunter College of the City University of New York, New York, N.Y. 10021. nucleic acid preparations (3,8,13). Nevertheless, the proper secondary structure of sRNA, essential for amino acid acceptor capacity (3), could be maintained at high temperatures in vivo by regulation of the polycation concentration (3,8).…”

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Stability of Ribosomes and Ribosomal Ribonucleic Acid from Bacillus stearothermophilus

1967

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After heating at 65 C, ribosomes isolated from Bacillus stearothermophilus were strikingly more heat-stable than comparable preparations from Escherichia coli when tested for ability to support polyuridylic acid-directed phenylalanine incorporation at 37 C. The stability of ribosomes was also determined by measurements of hyperchromicity at 259 m,u while heating them from 25 to 90 C. In standard buffer containing 0.01 M Mg+, the Tm (temperature at the midpoint of total hyperchromicity) of E. coli and B. stearothermophilus ribosomes was 71 and 81 C, respectively. In a magnesium-free buffer, the Tm of E. coli and B. stearothermophilus ribosomes was 44 and 64 C, respectively. Putrescine (0.01 M) was more effective in stabilizing ribosomes from B. stearothermophilus than those from E. coli. Spermidine (0.001 M), on the other hand, was more effective in stabilizing ribosomes from E. coli than those from B. stearothermophilus. Melting curves of total ribosomal ribonucleic acid (rRNA) from E. coli and B. stearothermophilus revealed Tm values of 50 and 60 C, respectively. Putrescine stabilized thermophile rRNA, but had no effect on E. coli rRNA. Sucrose density gradients demonstrated that thermophile 23S ribonucleic acid was degraded during storage at-20 C; the 23S component from E. coli was stable under these conditions. The results are discussed in terms ofthe mechanism of ribosome heat stability and the role of the ribosome in governing the temperature limits for bacterial growth.

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“…I hoped that the thermophilic microorganism Bacillus stearothermophilus, growing at temperatures up to 70°C, would be a source of factors stable for purification at lower temperatures (19). B. stearothermophilus turned out to be a good choice.…”

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confidence: 99%

Wanderings in Biochemistry

Lengyel

2014

Journal of Biological Chemistry

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Medicine in 1962 included the determination of the nucleotide compositions of codons specifying amino acids. The experiments were based on the use of random copolyribonucleotides (synthesized by polynucleotide phosphorylase) as messenger RNA in a cell-free protein-synthesizing system. At Yale University, where I joined the faculty, my co-workers and I first studied the mechanisms of protein synthesis. Thereafter, we explored the interferons (IFNs), which were discovered as antiviral defense agents but were revealed to be components of a highly complex multifunctional system. We isolated pure IFNs and characterized IFN-activated genes, the proteins they encode, and their functions. We concentrated on a cluster of IFN-activated genes, the p200 cluster, which arose by repeated gene duplications and which encodes a large family of highly multifunctional proteins. For example, the murine protein p204 can be activated in numerous tissues by distinct transcription factors. It modulates cell proliferation and the differentiation of a variety of tissues by binding to many proteins. p204 also inhibits the activities of wild-type Ras proteins and Ras oncoproteins.

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The enzymic synthesis of aminoacyl derivatives of soluble ribonucleic acid from Bacillus stearothermophilus

Cited by 7 publications

References 21 publications

Ribonucleic Acid and Ribosomes of Bacillus stearothermophilus

Ribonucleic Acid and Ribosomes of Bacillus stearothermophilus

Stability of Ribosomes and Ribosomal Ribonucleic Acid from Bacillus stearothermophilus

Wanderings in Biochemistry

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