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Originally published In Press as doi:10.1074/jbc.M203528200 on May 31, 2002

J. Biol. Chem., Vol. 277, Issue 33, 29537-29549, August 16, 2002
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The Sulfolobus solfataricus Lrp-like Protein LysM Regulates Lysine Biosynthesis in Response to Lysine Availability*

Arie B. BrinkmanDagger §, Stephen D. Bell, Robert Jan LebbinkDagger , 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 the  Medical Research Council Cancer Cell Unit, Hutchison MRC Centre, Hills Rd., Cambridge CB2 2XZ, United Kingdom

Although the archaeal transcription apparatus resembles the eukaryal RNA polymerase II system, many bacterial-like regulators can be found in archaea. Particularly, all archaeal genomes sequenced to date contain genes encoding homologues of Lrp (leucine-responsive regulatory protein). Whereas Lrp-like proteins in bacteria are involved in regulation of amino acid metabolism, their physiological role in archaea is unknown. Although several archaeal Lrp-like proteins have been characterized recently, no target genes apart from their own coding genes have been discovered yet, and no ligands for these regulators have been identified so far. In this study, we show that the Lrp-like protein LysM from Sulfolobus solfataricus is involved in the regulation of lysine and possibly also arginine biosynthesis, encoded by the lys gene cluster. Exogenous lysine is the regulatory signal for lys gene expression and specifically serves as a ligand for LysM by altering its DNA binding affinity. LysM binds directly upstream of the TFB-responsive element of the intrinsically weak lysW promoter, and DNA binding is favored in the absence of lysine, when lysWXJK transcription is maximal. The combined in vivo and in vitro data are most compatible with a model in which the bacterial-like LysM activates the eukarya-like transcriptional machinery. As with transcriptional activation by Escherichia coli Lrp, activation by LysM is apparently dependent on a co-activator, which remains to be identified.


* This research was supported by Council for Chemical Sciences of the Netherlands Organization for Scientific Research Grant 700-35-101.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: Dept. of Physiological Chemistry, University Medical Centre, P.O. Box 85060, 3508 AB Utrecht, The Netherlands. E-mail: a.b.brinkman@med.uu.nl.


Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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