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(Received for publication, June 13, 1996, and in revised form, August 7, 1996)
From the Department of Microbiology and Molecular Genetics, College
of Medicine, University of California, Irvine, California 92697
The leucine-responsive regulatory protein (Lrp)
regulates the expression of many operons in Escherichia coli
including several involved in the metabolism of the
branched-chain amino acids, L-isoleucine,
L-valine, and L-leucine. The ilvGMEDA
operon contains the genes for four of the five enzymes of the
common pathway for the biosynthesis of these amino acids. A high
affinity, consensus-like Lrp-DNA binding site has been identified at an
unusual position in the leader region of this operon 226 base pairs
downstream of the transcriptional initiation site between the
attenuator and the ilvG gene. Binding to this site
facilitates the cooperative binding of a second Lrp protomer to an
adjacent, upstream, secondary site. At higher Lrp concentrations,
binding to a third site is observed. Chemical, enzymatic, and
alkylation protection and interference footprinting experiments
demonstrate that the Lrp homodimer contacts the DNA helix at
symmetrical half-sites present in adjacent major grooves and that the
primary and secondary binding sites are separated by one helical turn
and aligned along the same face of the DNA helix. In vivo,
Lrp represses transcription through the leader-attenuator region
of the ilvGMEDA operon. Lrp-dependent
production of attenuated RNA transcripts is also observed in
vitro. No transcriptional effects are observed, in vivo
or in vitro, in the absence of an intact Lrp primary
binding site. A possible physiological role for Lrp in the regulation
of ilvGMEDA operon expression is discussed.
Volume 271, Number 43,
Issue of October 25, 1996
pp. 26499-26507
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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