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Journal of Bacteriology, March 1999, p. 1474-1480, Vol. 181, No. 5
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

An Lrp-Like Protein of the Hyperthermophilic Archaeon Sulfolobus solfataricus Which Binds to Its Own Promoterdagger

Alessandra Napoli,1 John van der Oost,2 Christoph W. Sensen,3 Robert L. Charlebois,4 Mosé Rossi,1 and Maria Ciaramella1,*

Institute of Protein Biochemistry and Enzymology, Consiglio Nazionale delle Ricerche, 80125 Naples, Italy1; Department of Microbiology, Wageningen Agricultural University, Wageningen 6703 CT, The Netherlands2; and Institute for Marine Biosciences, National Research Council of Canada, Halifax, NS, B3H 3Z1,3 and Department of Biology, University of Ottawa, Ottawa, Ontario K1N 6N54 Canada

Received 20 October 1998/Accepted 21 December 1998

Regulation of gene expression in the domain Archaea, and specifically hyperthermophiles, has been poorly investigated so far. Biochemical experiments and genome sequencing have shown that, despite the prokaryotic cell and genome organization, basal transcriptional elements of members of the domain Archaea (i.e., TATA box-like sequences, RNA polymerase, and transcription factors TBP, TFIIB, and TFIIS) are of the eukaryotic type. However, open reading frames potentially coding for bacterium-type transcription regulation factors have been recognized in different archaeal strains. This finding raises the question of how bacterial and eukaryotic elements interact in regulating gene expression in Archaea. We have identified a gene coding for a bacterium-type transcription factor in the hyperthermophilic archaeon Sulfolobus solfataricus. The protein, named Lrs14, contains a potential helix-turn-helix motif and is related to the Lrp-AsnC family of regulators of gene expression in the class Bacteria. We show that Lrs14, expressed in Escherichia coli, is a highly thermostable DNA-binding protein. Bandshift and DNase I footprint analyses show that Lrs14 specifically binds to multiple sequences in its own promoter and that the region of binding overlaps the TATA box, suggesting that, like the E. coli Lrp, Lrs14 is autoregulated. We also show that the lrs14 transcript is accumulated in the late growth stages of S. solfataricus.

* Corresponding author. Mailing address: Institute of Protein Biochemistry and Enzymology, Consiglio Nazionale delle Ricerche, Via Marconi 10, 80125 Naples, Italy. Phone: 39 081 7257 246. Fax: 39 081 239 6525. E-mail: ciaramel{at}dafne.ibpe.na.cnr.it.

dagger NRCC publication 42281.

Journal of Bacteriology, March 1999, p. 1474-1480, Vol. 181, No. 5
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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