This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Borges, K. M. Articles by Robb, F. T. Search for Related Content PubMed PubMed Citation Articles by Borges, K. M. Articles by Robb, F. T.

 Previous Article  |  Next Article 

J. Bacteriol., 03 1997, 1721-1726, Vol 179, No. 5
Copyright © 1997, American Society for Microbiology

Characterization of the reverse gyrase from the hyperthermophilic archaeon Pyrococcus furiosus

KM Borges, A Bergerat, AM Bogert, J DiRuggiero, P Forterre and FT Robb
Center of Marine Biotechnology, University of Maryland Biotechnology Institute, Baltimore, USA.

The reverse gyrase gene rgy from the hyperthermophilic archaeon Pyrococcus furiosus was cloned and sequenced. The gene is 3,642 bp (1,214 amino acids) in length. The deduced amino acid sequence has relatively high similarity to the sequences of the Methanococcus jannaschii reverse gyrase (48% overall identity), the Sulfolobus acidocaldarius reverse gyrase (41% identity), and the Methanopynrus kandleri reverse gyrase (37% identity). The P. furiosus reverse gyrase is a monomeric protein, containing a helicase-like module and a type I topoisomerase module, which resembles the enzyme from S. acidocaldarius more than that from M. kandleri, a heterodimeric protein encoded by two separate genes. The control region of the P. furiosus rgy gene contains a typical archaeal putative box A promoter element which is located at position -26 from the transcription start identified by primer extension experiments. The initiating ATG codon is preceded by a possible prokaryote-type ribosome-binding site. Purified P. furiosus reverse gyrase has a sedimentation coefficient of 6S, suggesting a monomeric structure for the native protein. The enzyme is a single polypeptide with an apparent molecular mass of 120 kDa, in agreement with the gene structure. The sequence of the N terminus of the protein corresponded to the deduced amino acid sequence. Phylogenetic analysis indicates that all known reverse gyrase topoisomerase modules form a subgroup inside subfamily IA of type I DNA topoisomerases (sensu Wang [J. C. Wang, Annu. Rev. Biochem. 65:635-692, 1996]). Our results suggest that the fusion between the topoisomerase and helicase modules of reverse gyrase occurred before the divergence of the two archaeal phyla, Crenoarchaeota and Euryarchaeota.

This article has been cited by other articles:

• Menon, A. L., Poole, F. L. II, Cvetkovic, A., Trauger, S. A., Kalisiak, E., Scott, J. W., Shanmukh, S., Praissman, J., Jenney, F. E. Jr., Wikoff, W. R., Apon, J. V., Siuzdak, G., Adams, M. W. W. (2009). Novel Multiprotein Complexes Identified in the Hyperthermophilic Archaeon Pyrococcus furiosus by Non-denaturing Fractionation of the Native Proteome. Mol. Cell. Proteomics 8: 735-751 [Abstract] [Full Text]  
• Hethke, C., Bergerat, A., Hausner, W., Forterre, P., Thomm, M. (1999). Cell-Free Transcription at 95{degrees}: Thermostability of Transcriptional Components and DNA Topology Requirements of Pyrococcus Transcription. Genetics 152: 1325-1333 [Abstract] [Full Text]  
• de la Tour, C. B., Portemer, C., Kaltoum, H., Duguet, M. (1998). Reverse Gyrase from the Hyperthermophilic Bacterium Thermotoga maritima: Properties and Gene Structure. J. Bacteriol. 180: 274-281 [Abstract] [Full Text]  
• Guipaud, O., Marguet, E., Noll, K. M., de la Tour, C. B., Forterre, P. (1997). Both DNA gyrase and reverse gyrase are present in the hyperthermophilic bacterium Thermotoga maritima. Proc. Natl. Acad. Sci. USA 94: 10606-10611 [Abstract] [Full Text]