Abstract
Protein turnover in the extreme bacterial thermophile Thermus aquaticus was examined in exponential cultures at 75 degrees C. The relative amount of [3H]leucine incorporated into trichloroacetic acid-insoluble material was stable in pulse-chase experiments assayed over 2.5 h. The trichloroacetic acid-insoluble radioactive leucine was stable upon the addition of chloramphenicol, which blocks protein synthesis in T. aquaticus. The specific activity of a phosphate-repressible alkaline phosphatase, investigated in the presence of chloramphenicol, did not decrease. The addition of excess orthophosphate to cultures derepressed for the alkaline phosphatase did not show a marked effect on the specific activity over a 2-h period. On the basis of these four experiments, it does not appear that a high protein turnover rate is essential for the thermophily of T. aquaticus at 75 degrees C.
Full text
PDF
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- ALLEN M. B. The thermophilic aerobic sporeforming bacteria. Bacteriol Rev. 1953 Jun;17(2):125–173. doi: 10.1128/br.17.2.125-173.1953. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Brock T. D., Freeze H. Thermus aquaticus gen. n. and sp. n., a nonsporulating extreme thermophile. J Bacteriol. 1969 Apr;98(1):289–297. doi: 10.1128/jb.98.1.289-297.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Brock T. D. Life at high temperatures. Evolutionary, ecological, and biochemical significance of organisms living in hot springs is discussed. Science. 1967 Nov;158(3804):1012–1019. doi: 10.1126/science.158.3804.1012. [DOI] [PubMed] [Google Scholar]
- Bubela B., Holdsworth E. S. Amino acid uptake, protein and nucleic acid synthesis and turnover in Bacillus stearothermophilus. Biochim Biophys Acta. 1966 Aug 17;123(2):364–375. doi: 10.1016/0005-2787(66)90289-9. [DOI] [PubMed] [Google Scholar]
- Castenholz R. W. Thermophilic blue-green algae and the thermal environment. Bacteriol Rev. 1969 Dec;33(4):476–504. doi: 10.1128/br.33.4.476-504.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gaughran E. R. THE THERMOPHILIC MICROORGANISMS. Bacteriol Rev. 1947 Sep;11(3):189–225. doi: 10.1128/br.11.3.189-225.1947. [DOI] [PMC free article] [PubMed] [Google Scholar]
- KOFFLER H. Protoplasmic differences between mesophiles and thermophiles. Bacteriol Rev. 1957 Dec;21(4):227–240. doi: 10.1128/br.21.4.227-240.1957. [DOI] [PMC free article] [PubMed] [Google Scholar]
- LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
- Nath K., Koch A. L. Protein degradation in Escherichia coli. I. Measurement of rapidly and slowly decaying components. J Biol Chem. 1970 Jun 10;245(11):2889–2900. [PubMed] [Google Scholar]
- Singleton R., Jr, Amelunxen R. E. Proteins from thermophilic microorganisms. Bacteriol Rev. 1973 Sep;37(3):320–342. doi: 10.1128/br.37.3.320-342.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Smile D. H., Donohue M., Yeh M. F., Kenkel T., Trela J. M. Repressible alkaline phosphatase from Thermus aquaticus: associated phosphodiesterase activity. J Biol Chem. 1977 May 25;252(10):3399–3401. [PubMed] [Google Scholar]
- Yeh M. F., Trela J. M. Purification and characterization of a repressible alkaline phosphatase from Thermus aquaticus. J Biol Chem. 1976 May 25;251(10):3134–3139. [PubMed] [Google Scholar]