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Microbiology 151 (2005), 763-773; DOI  10.1099/mic.0.27699-0
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Microbiology 151 (2005), 763-773; DOI  10.1099/mic.0.27699-0
© 2005 Society for General Microbiology

Analysis of ATPases of putative secretion operons in the thermoacidophilic archaeon Sulfolobus solfataricus

Sonja-Verena Albers and Arnold J. M. Driessen

Department of Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9751 NN Haren, The Netherlands

Correspondence
Arnold J. M. Driessen
a.j.m.driessen{at}biol.rug.nl

Gram-negative bacteria use a wide variety of complex mechanisms to secrete proteins across their membranes or to assemble secreted proteins into surface structures. As most archaea only possess a cytoplasmic membrane surrounded by a membrane-anchored S-layer, the organization of such complexes might be significantly different from that in Gram-negative bacteria. Five proteins of Sulfolobus solfataricus, SSO0120, SSO0572, SSO2316, SSO2387 and SSO2680, which are homologous to secretion ATPases of bacterial type II, type IV secretion systems and the type IV pili assembly machinery, were identified. The operon structures of these putative secretion systems encoding gene clusters and the expression patterns of the ATPases under different growth conditions were determined, and it was established that all five putative ATPases do show a divalent cation-dependent ATPase activity at high temperature. These results show that the archaeal secretion systems are related to the bacterial secretion systems and might be powered in a similar way.


Sequences of primers used to identify specific transcripts are listed in Supplementary Table S1 with the online version of this paper at http://mic.sgmjournals.org.




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