Skip to main content
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1990 Dec;172(12):6803–6808. doi: 10.1128/jb.172.12.6803-6808.1990

Reverse gyrase, a hallmark of the hyperthermophilic archaebacteria.

C Bouthier de la Tour 1, C Portemer 1, M Nadal 1, K O Stetter 1, P Forterre 1, M Duguet 1
PMCID: PMC210796  PMID: 2174859

Abstract

Investigation of the presence of a reverse gyrase-like activity in archaebacteria revealed wide distribution of this activity in hyperthermophilic species, including methanogens and sulfur-dependent organisms. In contrast, no reverse gyrase activity was detected in mesophilic and moderately thermophilic organisms, which exhibited only an ATP-independent activity of DNA relaxation. These results suggest that the presence of reverse gyrase in archaebacteria is tightly linked to the high growth temperatures of these organisms. With respect to antigenic properties, the enzyme appeared similar among members of the genus Sulfolobus. In contrast, no close antigenic relatedness was found between the reverse gyrase of members of the order Sulfolobales and that of the other hyperthermophilic organisms.

Full text

PDF
6803

Images in this article

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Achenbach-Richter L., Stetter K. O., Woese C. R. A possible biochemical missing link among archaebacteria. Nature. 1987 May 28;327(6120):348–349. doi: 10.1038/327348a0. [DOI] [PubMed] [Google Scholar]
  2. Barzilai R. SV40 DNA: quantitative conversion of closed circular to open circular form by an ethidium bromide-restricted endonuclease. J Mol Biol. 1973 Mar 15;74(4):739–742. doi: 10.1016/0022-2836(73)90062-4. [DOI] [PubMed] [Google Scholar]
  3. 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]
  4. Duguet M., Lavenot C., Harper F., Mirambeau G., De Recondo A. M. DNA topoisomerases from rat liver: physiological variations. Nucleic Acids Res. 1983 Feb 25;11(4):1059–1075. doi: 10.1093/nar/11.4.1059. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Fischer F., Zillig W., Stetter K. O., Schreiber G. Chemolithoautotrophic metabolism of anaerobic extremely thermophilic archaebacteria. Nature. 1983 Feb 10;301(5900):511–513. doi: 10.1038/301511a0. [DOI] [PubMed] [Google Scholar]
  6. Forterre P., Elie C., Sioud M., Hamal A. Studies on DNA polymerases and topoisomerases in archaebacteria. Can J Microbiol. 1989 Jan;35(1):228–233. doi: 10.1139/m89-035. [DOI] [PubMed] [Google Scholar]
  7. Forterre P., Mirambeau G., Jaxel C., Nadal M., Duguet M. High positive supercoiling in vitro catalyzed by an ATP and polyethylene glycol-stimulated topoisomerase from Sulfolobus acidocaldarius. EMBO J. 1985 Aug;4(8):2123–2128. doi: 10.1002/j.1460-2075.1985.tb03902.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Jaxel C., Nadal M., Mirambeau G., Forterre P., Takahashi M., Duguet M. Reverse gyrase binding to DNA alters the double helix structure and produces single-strand cleavage in the absence of ATP. EMBO J. 1989 Oct;8(10):3135–3139. doi: 10.1002/j.1460-2075.1989.tb08466.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Kikuchi A., Asai K. Reverse gyrase--a topoisomerase which introduces positive superhelical turns into DNA. Nature. 1984 Jun 21;309(5970):677–681. doi: 10.1038/309677a0. [DOI] [PubMed] [Google Scholar]
  10. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  11. Nadal M., Jaxel C., Portemer C., Forterre P., Mirambeau G., Duguet M. Reverse gyrase of Sulfolobus: purification to homogeneity and characterization. Biochemistry. 1988 Dec 27;27(26):9102–9108. doi: 10.1021/bi00426a006. [DOI] [PubMed] [Google Scholar]
  12. Nakasu S., Kikuchi A. Reverse gyrase; ATP-dependent type I topoisomerase from Sulfolobus. EMBO J. 1985 Oct;4(10):2705–2710. doi: 10.1002/j.1460-2075.1985.tb03990.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Schaffner W., Weissmann C. A rapid, sensitive, and specific method for the determination of protein in dilute solution. Anal Biochem. 1973 Dec;56(2):502–514. doi: 10.1016/0003-2697(73)90217-0. [DOI] [PubMed] [Google Scholar]
  14. Searcy D. G. Histone-like protein in the prokaryote Thermoplasma acidophilum. Biochim Biophys Acta. 1975 Jul 23;395(4):535–547. doi: 10.1016/0005-2787(75)90076-3. [DOI] [PubMed] [Google Scholar]
  15. Slesarev A. I. Positive supercoiling catalysed in vitro by ATP-dependent topoisomerase from Desulfurococcus amylolyticus. Eur J Biochem. 1988 Apr 15;173(2):395–399. doi: 10.1111/j.1432-1033.1988.tb14012.x. [DOI] [PubMed] [Google Scholar]
  16. Stetter K. O., Lauerer G., Thomm M., Neuner A. Isolation of extremely thermophilic sulfate reducers: evidence for a novel branch of archaebacteria. Science. 1987 May 15;236(4803):822–824. doi: 10.1126/science.236.4803.822. [DOI] [PubMed] [Google Scholar]
  17. Svoboda M., Meuris S., Robyn C., Christophe J. Rapid electrotransfer of proteins from polyacrylamide gel to nitrocellulose membrane using surface-conductive glass as anode. Anal Biochem. 1985 Nov 15;151(1):16–23. doi: 10.1016/0003-2697(85)90046-6. [DOI] [PubMed] [Google Scholar]
  18. Takahashi M., Yamaguchi E., Uchida T. Thermophilic DNA ligase. Purification and properties of the enzyme from Thermus thermophilus HB8. J Biol Chem. 1984 Aug 25;259(16):10041–10047. [PubMed] [Google Scholar]
  19. Woese C. R. Bacterial evolution. Microbiol Rev. 1987 Jun;51(2):221–271. doi: 10.1128/mr.51.2.221-271.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Woese C. R., Olsen G. J. Archaebacterial phylogeny: perspectives on the urkingdoms. Syst Appl Microbiol. 1986;7:161–177. doi: 10.1016/s0723-2020(86)80001-7. [DOI] [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES