Abstract
An alpha-amylase was purified from culture supernatants of Sulfolobus solfataricus 98/2 during growth on starch as the sole carbon and energy source. The enzyme is a homodimer with a subunit mass of 120 kDa. It catalyzes the hydrolysis of starch, dextrin, and alpha-cyclodextrin with similar efficiencies. Addition of exogenous glucose represses production of alpha-amylase, demonstrating that a classical glucose effect is operative in this organism. Synthesis of [35S]-alpha-amylase protein is also subject to the glucose effect. alpha-Amylase is constitutively produced at low levels but can be induced further by starch addition. The absolute levels of alpha-amylase detected in culture supernatants varied greatly with the type of sole carbon source used to support growth. Aspartate was identified as the most repressing sole carbon source for alpha-amylase production, while glutamate was the most derepressing. The pattern of regulation of alpha-amylase production seen in this organism indicates that a catabolite repression-like system is present in a member of the archaea.
Full Text
The Full Text of this article is available as a PDF (279.7 KB).
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- ALLEN M. B. Studies with Cyanidium caldarium, an anomalously pigmented chlorophyte. Arch Mikrobiol. 1959;32(3):270–277. doi: 10.1007/BF00409348. [DOI] [PubMed] [Google Scholar]
- Barns S. M., Fundyga R. E., Jeffries M. W., Pace N. R. Remarkable archaeal diversity detected in a Yellowstone National Park hot spring environment. Proc Natl Acad Sci U S A. 1994 Mar 1;91(5):1609–1613. doi: 10.1073/pnas.91.5.1609. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Brock T. D., Brock K. M., Belly R. T., Weiss R. L. Sulfolobus: a new genus of sulfur-oxidizing bacteria living at low pH and high temperature. Arch Mikrobiol. 1972;84(1):54–68. doi: 10.1007/BF00408082. [DOI] [PubMed] [Google Scholar]
- Brown S. H., Costantino H. R., Kelly R. M. Characterization of Amylolytic Enzyme Activities Associated with the Hyperthermophilic Archaebacterium Pyrococcus furiosus. Appl Environ Microbiol. 1990 Jul;56(7):1985–1991. doi: 10.1128/aem.56.7.1985-1991.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Costantino H. R., Brown S. H., Kelly R. M. Purification and characterization of an alpha-glucosidase from a hyperthermophilic archaebacterium, Pyrococcus furiosus, exhibiting a temperature optimum of 105 to 115 degrees C. J Bacteriol. 1990 Jul;172(7):3654–3660. doi: 10.1128/jb.172.7.3654-3660.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Epstein W., Rothman-Denes L. B., Hesse J. Adenosine 3':5'-cyclic monophosphate as mediator of catabolite repression in Escherichia coli. Proc Natl Acad Sci U S A. 1975 Jun;72(6):2300–2304. doi: 10.1073/pnas.72.6.2300. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Grogan D. W. Phenotypic characterization of the archaebacterial genus Sulfolobus: comparison of five wild-type strains. J Bacteriol. 1989 Dec;171(12):6710–6719. doi: 10.1128/jb.171.12.6710-6719.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Grogan D., Palm P., Zillig W. Isolate B12, which harbours a virus-like element, represents a new species of the archaebacterial genus Sulfolobus, Sulfolobus shibatae, sp. nov. Arch Microbiol. 1990;154(6):594–599. doi: 10.1007/BF00248842. [DOI] [PubMed] [Google Scholar]
- Hochstein L. I., Stan-Lotter H. Purification and properties of an ATPase from Sulfolobus solfataricus. Arch Biochem Biophys. 1992 May 15;295(1):153–160. doi: 10.1016/0003-9861(92)90501-m. [DOI] [PubMed] [Google Scholar]
- Hueck C. J., Hillen W. Catabolite repression in Bacillus subtilis: a global regulatory mechanism for the gram-positive bacteria? Mol Microbiol. 1995 Feb;15(3):395–401. doi: 10.1111/j.1365-2958.1995.tb02252.x. [DOI] [PubMed] [Google Scholar]
- Kurosawa N., Itoh Y. H. Nucleotide sequence of the 16S rRNA gene from thermoacidophilic archaea Sulfolobus acidocaldarius ATCC33909. Nucleic Acids Res. 1993 Jan 25;21(2):357–357. doi: 10.1093/nar/21.2.357. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Laderman K. A., Asada K., Uemori T., Mukai H., Taguchi Y., Kato I., Anfinsen C. B. Alpha-amylase from the hyperthermophilic archaebacterium Pyrococcus furiosus. Cloning and sequencing of the gene and expression in Escherichia coli. J Biol Chem. 1993 Nov 15;268(32):24402–24407. [PubMed] [Google Scholar]
- Laderman K. A., Davis B. R., Krutzsch H. C., Lewis M. S., Griko Y. V., Privalov P. L., Anfinsen C. B. The purification and characterization of an extremely thermostable alpha-amylase from the hyperthermophilic archaebacterium Pyrococcus furiosus. J Biol Chem. 1993 Nov 15;268(32):24394–24401. [PubMed] [Google Scholar]
- Leichtling B. H., Rickenberg H. V., Seely R. J., Fahrney D. E., Pace N. R. The occurrence of cyclic AMP in archaebacteria. Biochem Biophys Res Commun. 1986 May 14;136(3):1078–1082. doi: 10.1016/0006-291x(86)90443-2. [DOI] [PubMed] [Google Scholar]
- MAGASANIK B. Catabolite repression. Cold Spring Harb Symp Quant Biol. 1961;26:249–256. doi: 10.1101/sqb.1961.026.01.031. [DOI] [PubMed] [Google Scholar]
- MANNING G. B., CAMPBELL L. L. Thermostable alpha-amylase of Bacillus stearothermophilus. I. Crystallization and some general properties. J Biol Chem. 1961 Nov;236:2952–2957. [PubMed] [Google Scholar]
- Olsen G. J., Pace N. R., Nuell M., Kaine B. P., Gupta R., Woese C. R. Sequence of the 16S rRNA gene from the thermoacidophilic archaebacterium Sulfolobus solfataricus and its evolutionary implications. J Mol Evol. 1985;22(4):301–307. doi: 10.1007/BF02115685. [DOI] [PubMed] [Google Scholar]
- PARK J. T., JOHNSON M. J. A submicrodetermination of glucose. J Biol Chem. 1949 Nov;181(1):149–151. [PubMed] [Google Scholar]
- Rockabrand D., Arthur T., Korinek G., Livers K., Blum P. An essential role for the Escherichia coli DnaK protein in starvation-induced thermotolerance, H2O2 resistance, and reductive division. J Bacteriol. 1995 Jul;177(13):3695–3703. doi: 10.1128/jb.177.13.3695-3703.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rolfsmeier M., Blum P. Purification and characterization of a maltase from the extremely thermophilic crenarchaeote Sulfolobus solfataricus. J Bacteriol. 1995 Jan;177(2):482–485. doi: 10.1128/jb.177.2.482-485.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ronne H. Glucose repression in fungi. Trends Genet. 1995 Jan;11(1):12–17. doi: 10.1016/s0168-9525(00)88980-5. [DOI] [PubMed] [Google Scholar]
- Snowden L. J., Blumentals I. I., Kelly R. M. Regulation of Proteolytic Activity in the Hyperthermophile Pyrococcus furiosus. Appl Environ Microbiol. 1992 Apr;58(4):1134–1141. doi: 10.1128/aem.58.4.1134-1141.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Trumbly R. J. Glucose repression in the yeast Saccharomyces cerevisiae. Mol Microbiol. 1992 Jan;6(1):15–21. doi: 10.1111/j.1365-2958.1992.tb00832.x. [DOI] [PubMed] [Google Scholar]
- Woese C. R., Kandler O., Wheelis M. L. Towards a natural system of organisms: proposal for the domains Archaea, Bacteria, and Eucarya. Proc Natl Acad Sci U S A. 1990 Jun;87(12):4576–4579. doi: 10.1073/pnas.87.12.4576. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Zillig W. Confusion in the assignments of Sulfolobus sequences to Sulfolobus species. Nucleic Acids Res. 1993 Nov 11;21(22):5273–5273. doi: 10.1093/nar/21.22.5273. [DOI] [PMC free article] [PubMed] [Google Scholar]
- de Rosa M., Gambacorta A., Bu'lock J. D. Extremely thermophilic acidophilic bacteria convergent with Sulfolobus acidocaldarius. J Gen Microbiol. 1975 Jan;86(1):156–164. doi: 10.1099/00221287-86-1-156. [DOI] [PubMed] [Google Scholar]