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J. Biol. Chem., Vol. 277, Issue 33, 29537-29549, August 16, 2002
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From the 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.
The Sulfolobus solfataricus Lrp-like Protein
LysM Regulates Lysine Biosynthesis in Response to Lysine
Availability*
§,,, and
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
*
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.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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