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J. Biol. Chem., Vol. 276, Issue 3, 2098-2107, January 19, 2001
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From the Institute of Biochemistry and Biophysics, Polish Academy
of Sciences, 02-106 Warsaw, Poland
CysB is a tetrameric LysR-type transcriptional
regulator that acts as an activator of cys regulon genes
and as an autorepressor. Positive control of cys genes
requires the presence of the inducer N-acetylserine.
Following random and site-directed mutagenesis of the cysB
gene, 20 CysB variants were isolated. Six single amino acid
substitutions within the N terminus of CysB abolished the DNA-binding
ability of the protein. Seven mutations in the central region of CysB
affected its response to the inducer. Four of these CysB mutants
retained repressing activity, but lost their activating function
in vivo. Their DNA binding characteristics were consistent with an inability to respond to acetylserine by a qualitative change in
the DNA-protein interaction. Three of the single residue substitutions
resulted in constitutive activity of CysB. The electrophoretic mobility
of the complex formed by one of the CysBc variants with the
cysP promoter suggested a dimeric state of this protein.
Characteristics of six truncated CysB variants lacking 5-30 C-terminal
residues indicated the involvement of the C terminus in the DNA
binding, oligomerization, and stability of CysB. The single
substitution Y27G resulted in the CysBpc variant, able to
bind DNA and to respond to the inducer by a qualitative change in the
DNA-protein complex, but defective in the positive control of the
cysP promoter.
Functional Dissection of the LysR-type CysB Transcriptional
Regulator
REGIONS IMPORTANT FOR DNA BINDING, INDUCER RESPONSE,
OLIGOMERIZATION, AND POSITIVE CONTROL*
*
This work was supported in parts by grants from the Polish
State Committee for Scientific Research (Projects 6P04A03614 and 6P04A05216).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: Inst. of Biochemistry
and Biophysics, Polish Academy of Sciences, Pawinskiego 5A, 02-106 Warsaw, Poland. Tel.: 48-22-659-60-72 (ext. 1310); Fax: 48-39-12-16-23 or 48-22-658-46-36; E-mail: monikah@ibbrain.ibb.waw.pl.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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