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Originally published In Press as doi:10.1074/jbc.M005422200 on July 18, 2000

J. Biol. Chem., Vol. 275, Issue 41, 31624-31629, October 13, 2000
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Mechanism of Autoregulation by an Archaeal Transcriptional Repressor*

Stephen D. Bell and Stephen P. JacksonDagger

From the Wellcome Trust and Cancer Research Campaign Institute of Cancer and Developmental Biology, Cambridge CB2 1QR and Department of Zoology, University of Cambridge, Cambridge, CB2 3EJ, United Kingdom

The basal transcription machinery of archaea corresponds to the core components of the eucaryal RNA polymerase II apparatus. Thus, archaea possess a complex multi-subunit RNA polymerase, a TATA box-binding protein and a protein termed transcription factor B (TFB), which is a homologue of eucaryal transcription factor IIB (TFIIB). Intriguingly, archaeal genome sequencing projects have revealed the existence of homologues of bacterial transcriptional regulators. To investigate the mechanism of transcriptional regulation in archaea we have studied one such molecule, Lrs14, a Sulfolobus solfataricus P2 homologue of the bacterial leucine-responsive regulatory protein, Lrp. We find that purified Lrs14 specifically represses the transcription of its own gene in a reconstituted in vitro transcription system. Furthermore, we show that Lrs14 binding sites overlap the basal promoter elements of the Lrs14 promoter and reveal that binding of Lrs14 to these sites prevents promoter recognition by TATA box-binding protein and TFB.

* This work was supported by the Wellcome Trust.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.

Dagger To whom correspondence should be addressed: The Wellcome Trust and Cancer Research Campaign Inst. of Cancer and Developmental Biology, Tennis Court Road, Cambridge, CB2 1QR, UK. Tel.: 01223-334102 or 331725; Fax: 01223-334089; E-mail: spj13@mole.bio.cam.ac.uk.

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