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Originally published In Press as doi:10.1074/jbc.M005916200 on September 5, 2000

J. Biol. Chem., Vol. 275, Issue 49, 38160-38169, December 8, 2000
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An Lrp-like Transcriptional Regulator from the Archaeon Pyrococcus furiosus Is Negatively Autoregulated*

Arie B. BrinkmanDagger §, Isabell Dahlke, Judith E. TuiningaDagger , Torsten Lammers, Valerie DumayDagger , Edwin de HeusDagger , Joyce H. G. LebbinkDagger , Michael Thomm, Willem M. de VosDagger , and John van der OostDagger

From the Dagger  Laboratory of Microbiology, Department of Agrotechnology and Food Sciences, Wageningen University, Hesselink van Suchtelenweg 4, 6703 CT Wageningen, The Netherlands and  Institut für Allgemeine Mikrobiologie, Cristian-Albrechts Universität zu Kiel, Am Botanischen Garten 1-9, 24118 Kiel, Germany

The archaeal transcriptional initiation machinery closely resembles core elements of the eukaryal polymerase II system. However, apart from the established basal archaeal transcription system, little is known about the modulation of gene expression in archaea. At present, no obvious eukaryal-like transcriptional regulators have been identified in archaea. Instead, we have previously isolated an archaeal gene, the Pyrococcus furiosus lrpA, that potentially encodes a bacterial-like transcriptional regulator. In the present study, we have for the first time addressed the actual involvement of an archaeal Lrp homologue in transcription modulation. For that purpose, we have produced LrpA in Escherichia coli. In a cell-free P. furiosus transcription system we used wild-type and mutated lrpA promoter fragments to demonstrate that the purified LrpA negatively regulates its own transcription. In addition, gel retardation analyses revealed a single protein-DNA complex, in which LrpA appeared to be present in (at least) a tetrameric conformation. The location of the LrpA binding site was further identified by DNaseI and hydroxyl radical footprinting, indicating that LrpA binds to a 46-base pair sequence that overlaps the transcriptional start site of its own promoter. The molecular basis of the transcription inhibition by LrpA is discussed.

* This research was supported by Council for Chemical Sciences (CW) of the Netherlands Organization for Scientific Research (NWO) Grant 700-35-101 and by grants of the Deutsche Forschungsgemeinschaft and the Fonds der Chemischen Industrie to (to M. T.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ To whom correspondence should be addressed: Laboratory of Microbiology, Dept. of Agrotechnology and Food Sciences, Wageningen University, Hesselink van Suchtelenweg 4, 6703 CT Wageningen, The Netherlands. Tel.: 0031-317-483110; Fax: 0031-317-483829; E-mail: arjen.brinkman@algemeen.micr.wau.nl.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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